40 results on '"F. Javier Gella"'
Search Results
2. Nomenclatura y unidades de las propiedades biológicas. Recomendación (2016)
- Author
-
M. Jesús Andrés Otero, Ruth Cano Corres, Francesca Canalias Reverter, Rosa M. López Martínez, Sara Esteve Poblador, F. Javier Gella Tomás, Bernardino González de la Presa, Raúl Rigo Bonnin, and Inmaculada Pérez de Algaba
- Subjects
Engineering ,010405 organic chemistry ,business.industry ,Biochemistry (medical) ,Clinical Biochemistry ,010402 general chemistry ,business ,01 natural sciences ,0104 chemical sciences - Published
- 2018
- Full Text
- View/download PDF
3. Validación de procedimientos de medida basados en la cromatografía líquida de alta resolución
- Author
-
Francesca Canalias Reverter, Rosa M. López Martínez, Sara Esteve Poblador, Bernardino González de la Presa, Raúl Rigo Bonnin, and F. Javier Gella Tomás
- Subjects
030213 general clinical medicine ,03 medical and health sciences ,0302 clinical medicine ,010405 organic chemistry ,Chemistry ,Biochemistry (medical) ,Clinical Biochemistry ,01 natural sciences ,0104 chemical sciences - Published
- 2018
- Full Text
- View/download PDF
4. Procedimiento para la transferencia y revisión de intervalos de referencia biológicos
- Author
-
Bernardino González de la Presa, Núria Serrat Orús., Rosa M. López Martínez, Francesca Canalias Reverter, F. Javier Gella Tomás, Raúl Rigo Bonnin, Silvia Izquierdo Álvarez, and Sara Esteve Poblador
- Subjects
Biochemistry (medical) ,Clinical Biochemistry ,Mathematics - Published
- 2017
- Full Text
- View/download PDF
5. Evaluación multicéntrica de materiales para el control de calidad de los índices séricos
- Author
-
Albert Blanco, F. Javier Gella, Josep Torres, Joaquim Ruiz, Virtudes Alvarez, Margarita Simón, Nuria Serrat, Carmen Biosca, Mercè Ibarz, Maribel Sánchez, M. Jesús Alsina, Mercè Montesinos, and Maribel Llovet
- Subjects
Biochemistry (medical) ,Clinical Biochemistry - Abstract
Resumen Introduccion La hemolisis, la turbidez y la presencia de concentraciones elevadas de bilirrubina son las fuentes de interferencia mas frecuentes en el laboratorio clinico. Muchos analizadores incorporan sistemas de deteccion de estos interferentes denominados «indices sericos» de hemolisis, ictericia y lipidemia. El grado de veracidad de los indices no suele ser verificado por la dificultad en conseguir materiales de referencia adecuados. En este trabajo se presentan los resultados de un estudio interlaboratorios de los indices hemolisis, ictericia y lipidemia empleando materiales de referencia con concentraciones conocidas de los interferentes. Material y metodos En el estudio han participado los laboratorios clinicos de 10 centros con 7 analizadores distintos. Los materiales de referencia de indices sericos contenian concentraciones conocidas de bilirrubina, hemoglobina (hemolisado) y trigliceridos (Intralipid). Resultados Todos los instrumentos proporcionaron resultados aceptables para el indice de ictericia y de hemolisis. Entre los analizadores que dan valores cuantitativos se encontraron resultados bajos en uno de los analizadores para los materiales que contenian Intralipid. Los analizadores que expresan el resultado en forma de un intervalo proporcionaron resultados correctos para los materiales con turbidez menor y bajos para el material con turbidez mayor. Conclusiones Los materiales de referencia utilizados han demostrado su utilidad para verificar los indices sericos de ictericia, hemolisis y lipidemia en los analizadores. Generalmente los indices proporcionados por los instrumentos concuerdan entre si y con los valores asignados. Las diferencias mas importantes entre analizadores se encuentran en el indice de lipidemia.
- Published
- 2015
- Full Text
- View/download PDF
6. Evaluación multicéntrica del nuevo sistema analítico BioSystems BA 400® y comparación de procedimientos de medida
- Author
-
Dolors Pelegrí Santos, Immaculada Comas Reixach, Bernardino González De La Presa, F. Javier Gella Tomás, Jaume Mont Borrell, Sergi Tortosa Morist, Dolors Dot Bach, Javier Sánchez Álvarez, and Blai Morales Romero
- Subjects
Biochemistry (medical) ,Clinical Biochemistry - Abstract
Resumen Objetivo El objetivo de este trabajo fue evaluar, mediante un estudio multicentrico, la imprecision y la veracidad de un elevado numero de procedimientos de medida en el nuevo sistema analitico BioSystems BA 400 ® . Material y metodo El estudio de la imprecision se llevo a cabo siguiendo recomendaciones establecidas y utilizando sueros control con 2 concentraciones distintas. El estudio de la veracidad se ha realizado mediante la comparacion de los procedimientos de medida del nuevo sistema con los utilizados habitualmente en los centros evaluadores. Resultados Los resultados obtenidos para la imprecision interdiaria con el nuevo analizador han sido en general excelentes en relacion a los errores maximos permitidos. Se han encontrado algunas diferencias no despreciables y estadisticamente significativas entre los distintos procedimientos de medida, que son debidas a diferencias en el mensurando en algunos casos (transaminasas, inmunoanalisis) y a diferencias en los calibradores en otros. Conclusiones La evaluacion ha demostrado las excelentes prestaciones de precision y veracidad del sistema. El nuevo analizador proporciona resultados en muestras de pacientes que son equivalentes a los obtenidos con otros analizadores (Olympus AU5400 y AU2700, Roche Cobas C711 y Siemens ADVIA 2400, 1800 y BNII).
- Published
- 2013
- Full Text
- View/download PDF
7. Traceability of values for catalytic activity concentration of enzymes: a Certified Reference Material for aspartate transaminase
- Author
-
Heinz Schimmel, Poul J. Jørgensen, Francesca Canalias, Georges Férard, F. Javier Gella, Joseph Henny, Shigeru Ueda, Mauro Panteghini, Daniel Mazziotta, Rainer Klauke, Hendrik Emons, Brigitte Toussaint, Jean Marc Lessinger, Steffen Dipl C Bossert-Reuther, Gerhard Schumann, Ferruccio Ceriotti, Carlo A. Ferrero, and Paul F H Franck
- Subjects
Clinical Biochemistry ,Aspartate transaminase ,Human type ,Liver enzyme ,Animals ,Humans ,Medicine ,Aspartate Aminotransferases ,chemistry.chemical_classification ,Chromatography ,biology ,business.industry ,Biochemistry (medical) ,Uncertainty ,Serum Albumin, Bovine ,General Medicine ,Clinical Enzyme Tests ,Reference Standards ,Recombinant Proteins ,Enzyme ,Certified reference materials ,Biochemistry ,chemistry ,biology.protein ,Cattle ,Coverage factor ,business - Abstract
Background: A new reference material for the liver enzyme aspartate transaminase (AST) (L-aspartate: 2-oxoglutarate-aminotransferase, EC 2.6.1.1), also called aspartate aminotransferase (ASAT), has been developed under the code ERM-AD457/IFCC. This certified reference material (CRM) for AST has been produced from a human type recombinant AST expressed in Escherichia coli and a buffer containing bovine serum albumin, and has been lyophilised. Methods: The homogeneity and the stability of the material have been tested and the catalytic activity concentration has been characterised by 12 laboratories using the reference procedure for AST at 37°C from the International Federation of Clinical Chemistry and Laboratory Medicine (IFCC). Results: The certified catalytic activity concentration and certified uncertainty of AST in the reconstituted material are (1.74±0.05) μkat/L or (104.6±2.7) U/L (with a coverage factor k=2; 95% confidence interval). Conclusions: Both the certified value and uncertainty are traceable to the International System of Units (SI). The material is aiming to control the IFCC reference procedure for AST at 37°C, which will then be used to assign values to calibrants and control materials. The present paper highlights the scientific challenges and innovations which were encountered during the development of this new CRM. Clin Chem Lab Med 2010;48:795–803.
- Published
- 2010
- Full Text
- View/download PDF
8. Production and certification of an enzyme reference material for adenosine deaminase 1 (BCR 647)
- Author
-
Francesca Canalias, Mogens Hørder, Alexandre Bota, F. Javier Gella, Rosa Segura, Françoise Schiele, Anthony G. Hadjivassiliou, Christos Profilis, and Georges Férard
- Subjects
Adenosine Deaminase ,Clinical Biochemistry ,Dehydrogenase ,Biochemistry ,Catalysis ,Adenosine deaminase ,Enzyme Stability ,medicine ,Humans ,Enzyme measurements ,Polyacrylamide gel electrophoresis ,chemistry.chemical_classification ,Chromatography ,biology ,Chemistry ,Glutamate dehydrogenase ,Biochemistry (medical) ,General Medicine ,Reference Standards ,Human serum albumin ,Adenosine ,Isoelectric point ,Enzyme ,biology.protein ,Reference material ,Standardisation ,medicine.drug - Abstract
Background: We describe the preparation of a lyophilised reference material containing purified human adenosine deaminase 1 and the certification of its catalytic concentration. Methods: The enzyme was purified from human erythrocytes. Results: The enzyme was >99% pure on polyacrylamide gel electrophoresis. Only trace amounts (
- Published
- 2001
- Full Text
- View/download PDF
9. Purification of human adenosine deaminase for the preparation of a reference material
- Author
-
Francesca Canalias, F. Javier Gella, and Alexandre Bota
- Subjects
chemistry.chemical_classification ,Chromatography ,biology ,Adenosine Deaminase ,Catalytic concentration ,Isoelectric focusing ,Blotting, Western ,General Chemistry ,Single band ,Reference Standards ,Chromatography, Ion Exchange ,Chromatography, Affinity ,Electrophoresis ,Red blood cell ,Enzyme ,medicine.anatomical_structure ,Adenosine deaminase ,Biochemistry ,chemistry ,medicine ,biology.protein ,Humans ,Electrophoresis, Polyacrylamide Gel ,Specific activity ,Isoelectric Focusing - Abstract
The goal was to optimise a purification procedure of adenosine deaminase from human erythrocytes for the preparation of a European Reference Material. Adenosine deaminase was purified from human erythrocytes with a specific activity of 4.46 microkat/mg of protein and a catalytic concentration of 133 microkat/l. The isolation and purification procedure involved ion-exchange chromatography (STREAMLINE DEAE), and two purine riboside affinity chromatographies. The purified enzyme exhibits a single band in SDS-PAGE with a molecular weight of 41600 g/mol, and three bands in PAGE, isoelectric focusing and two-dimensional electrophoresis with pI 4.7, 4.85 and 5.0.
- Published
- 2000
- Full Text
- View/download PDF
10. Production and certification of an enzyme reference material for pancreatic α-amylase (CRM 476)
- Author
-
Elizabeth Colinet, D.H. Calam, J. Dufaux, Anne Vassault, Klaus Lorentz, F. Javier Gella, Francesca Canalias, Christos Profilis, Jean Marc Lessinger, Ferruccio Ceriotti, Anthony G. Hadjivassiliou, and Gemma Gubern
- Subjects
Time Factors ,Sodium ,Clinical Biochemistry ,chemistry.chemical_element ,Biochemistry ,Catalysis ,Drug Stability ,medicine ,Humans ,Amylase ,Lipase ,Pancreas ,Polyacrylamide gel electrophoresis ,Chromatography ,biology ,Biochemistry (medical) ,General Medicine ,Hydrogen-Ion Concentration ,Reference Standards ,Human serum albumin ,Enzyme assay ,Freeze Drying ,Isoelectric point ,chemistry ,Sephadex ,biology.protein ,Electrophoresis, Polyacrylamide Gel ,Indicators and Reagents ,Spectrophotometry, Ultraviolet ,alpha-Amylases ,medicine.drug - Abstract
We describe the preparation of a lyophilized material containing purified human pancreatic alpha-amylase and the certification of its catalytic concentration. The enzyme was purified from human pancreas by ammonium sulphate precipitation and chromatography successively on DEAE-Sephacel, CM-Sepharose and Sephadex G-75. The purified enzyme had a specific activity of 52.9 kU/g protein and was99% pure on polyacrylamide gel electrophoresis. Only trace amounts of lipase and lactate dehydrogenase were detected in the purified fraction. The purified pancreatic alpha-amylase had a molar mass of 57,500 g/mol and an isoelectric point at 7.1. The material was prepared by diluting the purified alpha-amylase in a matrix containing PIPES buffer 25 mmol/l, pH 7.0, sodium chloride 50 mmol/l, calcium chloride 1.5 mmol/l, EDTA 0.5 mmol/l and human serum albumin 30 g/l, dispensing in ampoules and freeze-drying. The ampoules were homogeneous and the yearly loss of activity on the basis of accelerated degradation studies was less than 0.01% at -20 degrees C. The certified value for alpha-amylase catalytic concentration in the reconstituted reference material is 555 U/l +/- 11 U/l when measured by the specified method at 37 degrees C. The material can be used to verify the comparability of results from laboratories, for intra-laboratory quality control or for calibration of alpha-amylase catalytic concentration measurements.
- Published
- 1996
- Full Text
- View/download PDF
11. IFCC primary reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 °C. Part 9: reference procedure for the measurement of catalytic concentration of alkaline phosphatase International Federation of Clinical Chemistry and Laboratory Medicine (IFCC) Scientific Division, Committee on Reference Systems of Enzymes (C-RSE) (1))
- Author
-
Gerhard, Schumann, Rainer, Klauke, Francesca, Canalias, Steffen, Bossert-Reuther, Paul F H, Franck, F-Javier, Gella, Poul J, Jørgensen, Dongchon, Kang, Jean-Marc, Lessinger, Mauro, Panteghini, and Ferruccio, Ceriotti
- Subjects
Adult ,Male ,Adolescent ,Temperature ,International Agencies ,Hydrogen-Ion Concentration ,Middle Aged ,Reference Standards ,Alkaline Phosphatase ,Enzymes ,Solutions ,Young Adult ,Research Design ,Calibration ,Humans ,Female ,Enzyme Assays - Abstract
This paper is the ninth in a series dealing with reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 °C and the certification of reference preparations. Other parts deal with: Part 1. The concept of reference procedures for the measurement of catalytic activity concentrations of enzymes; Part 2. Reference procedure for the measurement of catalytic concentration of creatine kinase; Part 3. Reference procedure for the measurement of catalytic concentration of lactate dehydrogenase; Part 4. Reference procedure for the measurement of catalytic concentration of alanine aminotransferase; Part 5. Reference procedure for the measurement of catalytic concentration of aspartate aminotransferase; Part 6. Reference procedure for the measurement of catalytic concentration of γ-glutamyltransferase; Part 7. Certification of four reference materials for the determination of enzymatic activity of γ-glutamyltransferase, lactate dehydrogenase, alanine aminotransferase and creatine kinase at 37 °C; Part 8. Reference procedure for the measurement of catalytic concentration of α-amylase. The procedure described here is derived from the previously described 30 °C IFCC reference method. Differences are tabulated and commented on in Appendix 1.
- Published
- 2011
12. IFCC primary reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 °C. Part 9: Reference procedure for the measurement of catalytic concentration of alkaline phosphatase
- Author
-
Mauro Panteghini, Poul J. Jørgensen, F-Javier Gella, Jean-Marc Lessinger, Gerhard Schumann, Paul F H Franck, Dongchon Kang, Steffen Dipl C Bossert-Reuther, Rainer Klauke, Francesca Canalias, and Ferruccio Ceriotti
- Subjects
chemistry.chemical_classification ,Chromatography ,Catalytic concentration ,Biochemistry (medical) ,Clinical Biochemistry ,General Medicine ,Reference intervals ,Catalysis ,chemistry.chemical_compound ,Enzyme ,Chemical engineering ,chemistry ,Lactate dehydrogenase ,Alkaline phosphatase ,Alanine aminotransferase ,Reference standards - Abstract
This paper is the ninth in a series dealing with reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 °C and the certification of reference preparations. Other parts deal with: Part 1. The concept of reference procedures for the measurement of catalytic activity concentrations of enzymes; Part 2. Reference procedure for the measurement of catalytic concentration of creatine kinase; Part 3. Reference procedure for the measurement of catalytic concentration of lactate dehydrogenase; Part 4. Reference procedure for the measurement of catalytic concentration of alanine aminotransferase; Part 5. Reference procedure for the measurement of catalytic concentration of aspartate aminotransferase; Part 6. Reference procedure for the measurement of catalytic concentration of γ-glutamyltransferase; Part 7. Certification of four reference materials for the determination of enzymatic activity of γ-glutamyltransferase, lactate dehydrogenase, alanine aminotransferase and creatine kinase at 37 °C; Part 8. Reference procedure for the measurement of catalytic concentration of α-amylase. The procedure described here is derived from the previously described 30 °C IFCC reference method. Differences are tabulated and commented on in Appendix 1.
- Published
- 2011
- Full Text
- View/download PDF
13. Latex agglutination procedures in immunodiagnosis
- Author
-
F. Javier Gella, Juan Gener, and J. Serra
- Subjects
Analyte ,Agglutination (biology) ,Chromatography ,Chemistry ,General Chemical Engineering ,Chemical groups ,General Chemistry ,Latex fixation test - Abstract
Latex agglutination tests have been in use since 1956 to detect a wide range of analytes in the clinical labo- ratory. When spectrophotometers and nephelometers are used in place of the human eye to detect agglutination, it is possible to measure quantitatively and to develop sensitive particle immunoassays. Latex particles may be build from different or- ganic materials to a desired diameter, and may be functionali- zed with chemical groups to facilitate attachment of molecules Proteins and other molecules may be passively adsorbed to the latex particles or covalently coupled to functional groups. Some described automated latex agglutination tests have sensi- tivities of a few picograms of analyte.
- Published
- 1991
- Full Text
- View/download PDF
14. Purification and characterization of native and proteolytic forms of rabbit liver phosphorylase kinase
- Author
-
Pilar Benedicto, F. Javier Gella, Pere Aymerich, and Jorge Beleta
- Subjects
Macromolecular Substances ,Phosphorylase Kinase ,Size-exclusion chromatography ,Biochemistry ,Antibodies ,Chromatography, Affinity ,chemistry.chemical_compound ,Adenosine Triphosphate ,Affinity chromatography ,medicine ,Animals ,Magnesium ,Sodium dodecyl sulfate ,Phosphorylase kinase ,Magnesium ion ,Chromatography ,Chymotrypsin ,biology ,Chemistry ,Muscles ,Hydrogen-Ion Concentration ,Trypsin ,Molecular Weight ,Kinetics ,Liver ,Chromatography, Gel ,biology.protein ,Sodium Fluoride ,Electrophoresis, Polyacrylamide Gel ,Rabbits ,Ultracentrifugation ,Peptide Hydrolases ,Homogenization (biology) ,medicine.drug - Abstract
1. 1. Two forms of phosphorylase kinase having mol. wt of 1,260,000 (form I) and 205,000 (form II) have been identified by gel filtration chromatography of rabbit liver crude extracts. 2. 2. Form I was the majority when the homogenization buffer was supplemented with a mixture of proteinase inhibitors. This form has been purified through a protocol including ultracentrifugation, gel filtration and affinity chromatography on Sepharose-heparin. 3. 3. Form II was purified by a combination of chromatographic procedures including ion exchange, gel filtration and affinity chromatography on Sepharose-Blue Dextran and Sepharose-histone. 4. 4. Upon electrophoresis in the presence of sodium dodecyl sulfate two subunits of 69,000 and 44,000 were identified for this low molecular weight enzyme. Thus, a tetrameric structure comprising two subunits of each kind can be proposed. 5. 5. Treatment of form I with either trypsin or chymotrypsin gave an active fragment having a molecular weight similar to that of form II. On the contrary, other dissociating treatments with salts, thiols and detergents failed in producing forms of lower molecular weight. 6. 6. The similarities between proteolyzed forms I and II were stressed by their behavior in front of antibodies raised against the muscle isoenzyme of phosphorylase kinase. 7. 7. The study of the effect of magnesium and fluoride ions on the activity of both forms showed an inhibitory effect of magnesium when its concentration exceeded that of ATP. 8. 8. The inhibition could nevertheless be reverted by including 50 mM NaF in the reaction mixture. 9. 9. Form I and form II could be distinguished by their pH dependence in the presence of an excess of magnesium ions over ATP, whereas the affinity for both substrates was not significantly different.
- Published
- 1990
- Full Text
- View/download PDF
15. Regulatory properties of rabbit liver phosphorylase kinase
- Author
-
Jorge Beleta, F. Javier Gella, and Pilar Benedicto
- Subjects
Phosphorylase Kinase ,Mitogen-activated protein kinase kinase ,Biology ,MAP3K7 ,Biochemistry ,MAP2K7 ,Adenosine Triphosphate ,Protein Phosphatase 1 ,Cyclic AMP ,Phosphoprotein Phosphatases ,Animals ,Magnesium ,Phosphorylation ,Phosphorylase kinase ,Protein kinase A ,Cyclin-dependent kinase 3 ,Enzyme Activation ,Molecular Weight ,Kinetics ,Liver ,Cyclin-dependent kinase complex ,Calcium ,Rabbits ,Protein Kinases ,cGMP-dependent protein kinase - Abstract
1. 1. Purified native rabbit liver phosphorylase kinase becomes activated during the assay of its activity while low molecular weight forms of the same enzyme do not. 2. 2. The activation requires ATP and maganesium ions, suggesting the phosphorylation of the enzyme by a protein kinase as the mechanism involved. 3. 3. The activation of the enzyme can be reverted by the action of a type 1 protein phosphatase isolated from the same tissue. 4. 4. The activation can also be catalyzed by the catalytic subunit of cAMP-dependent protein kinase in a process that requires a much lower ATP concentration to proceed. 5. 5. The activation is believed to be due to an autocatalytic phosphorylation of phosphorylase kinase itself. In support of this hypothesis are the regulation of the process through calcium ions, the low levels of endogenous protein kinase detected in the purified preparation, the high ATP concentrations required in the absence of cAMP dependent protein kinase and the fact that the process cannot be blocked by an excess of the heat stable inhibitor specific for the later enzyme. 6. 6. The low molecular weight forms of the enzyme on their side are not affected by the action of neither protein phosphatase 1 nor cyclic AMP dependent protein kinase. 7. 7. Both activated and nonactivated phosphorylase kinase are partially dependent on calcium ions, the affinity of the former being higher than that of the latter. The low molecular forms do not require calcium ions to express their activity.
- Published
- 1990
- Full Text
- View/download PDF
16. IFCC primary reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C
- Author
-
Gerhard, Schumann, Ryoji, Aoki, Carlo A, Ferrero, Glenn, Ehlers, Georges, Férard, F-Javier, Gella, Poul Jørgen, Jørgensen, Takahashi, Kanno, Art, Kessner, Rainer, Klauke, Hans-Joachim, Kytzia, Jean-Marc, Lessinger, W Gregory, Miller, Rolf, Nagel, Jean, Pauwels, Heinz, Schimmel, Lothar, Siekmann, Gerhard, Weidemann, Kyoshi, Yoshida, and Ferruccio, Ceriotti
- Subjects
Kinetics ,L-Lactate Dehydrogenase ,Reference Values ,Enzyme Stability ,Temperature ,Alanine Transaminase ,Glycoside Hydrolase Inhibitors ,alpha-Glucosidases ,gamma-Glutamyltransferase ,Clinical Enzyme Tests ,Hydrogen-Ion Concentration ,Creatine Kinase ,Catalysis - Abstract
This paper is the eighth in a series dealing with reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C and the certification of reference preparations. Other parts deal with: Part 1. The concept of reference procedures for the measurement of catalytic activity concentrations of enzymes; Part 2. Reference procedure for the measurement of catalytic concentration of creatine kinase; Part 3. Reference procedure for the measurement of catalytic concentration of lactate dehydrogenase; Part 4. Reference procedure for the measurement of catalytic concentration of alanine aminotransferase Part 5. Reference procedure for the measurement of catalytic concentration of aspartate aminotransferase Part 6. Reference procedure for the measurement of catalytic concentration of gamma-glutamyltransferase; Part 7. Certification of four reference materials for the determination of enzymatic activity of gamma-glutamyltransferase, lactate dehydrogenase, alanine aminotransferase and creatine kinase at 37 degrees C. The procedure described here is deduced from the previously described 30 degrees C IFCC reference method. Differences are tabulated and commented on.
- Published
- 2006
17. IFCC primary reference procedures for the measurement of catalytic activity concentrations of enzymes at 37°C: International Federation of Clinical Chemistry and Laboratory Medicine (IFCC): Scientific Division, Committee on Reference Systems for Enzymes (C-RSE): Part 8. Reference procedure for the measurement of catalytic concentration of α-amylase: [α-Amylase: 1,4-α-D-glucan 4-glucanohydrolase (AMY), EC 3.2.1.1]
- Author
-
Ferruccio Ceriotti, Georges Férard, Poul J. Jørgensen, T Kanno, Carlo A. Ferrero, F-Javier Gella, Hans-Joachim Kytzia, Ryoji Aoki, Gerhard Schumann, Rolf Nagel, A Kessner, Jean-Marc Lessinger, Jean Pauwels, W. Gregory Miller, Rainer Klauke, Gerhard Weidemann, Glenn W. Ehlers, Lothar Siekmann, Kyoshi Yoshida, and Heinz Schimmel
- Subjects
chemistry.chemical_classification ,Chromatography ,biology ,Catalytic concentration ,Biochemistry (medical) ,Clinical Biochemistry ,General Medicine ,Catalysis ,chemistry.chemical_compound ,Enzyme ,chemistry ,Chemical engineering ,Reference values ,Lactate dehydrogenase ,biology.protein ,Creatine kinase ,Alanine aminotransferase - Abstract
This paper is the eighth in a series dealing with reference procedures for the measurement of catalytic activity concentrations of enzymes at 37°C and the certification of reference preparations. Other parts deal with: Part 1. The concept of reference procedures for the measurement of catalytic activity concentrations of enzymes; Part 2. Reference procedure for the measurement of catalytic concentration of creatine kinase; Part 3. Reference procedure for the measurement of catalytic concentration of lactate dehydrogenase; Part 4. Reference procedure for the measurement of catalytic concentration of alanine aminotransferase Part 5. Reference procedure for the measurement of catalytic concentration of aspartate aminotransferase Part 6. Reference procedure for the measurement of catalytic concentration of γ-glutamyltransferase; Part 7. Certification of four reference materials for the determination of enzymatic activity of γ-glutamyltransferase, lactate dehydrogenase, alanine aminotransferase and creatine kinase at 37°C. The procedure described here is deduced from the previously described 30°C IFCC reference method. Differences are tabulated and commented on.Clin Chem Lab Med 2006;44:1146–55.
- Published
- 2006
- Full Text
- View/download PDF
18. Metrological traceability of values for catalytic concentration of enzymes assigned to a calibration material
- Author
-
F-Javier Gella, Maribel Sánchez, Sandra Camprubí, and Francesca Canalias
- Subjects
Quality Control ,Traceability ,Catalytic concentration ,Clinical Biochemistry ,Metrological traceability ,Analytical chemistry ,Guidelines as Topic ,Catalysis ,Units of measurement ,Reference Values ,Calibration ,Humans ,Creatine Kinase ,Chromatography ,L-Lactate Dehydrogenase ,Chemistry ,Biochemistry (medical) ,Reproducibility of Results ,Alanine Transaminase ,gamma-Glutamyltransferase ,General Medicine ,Clinical Enzyme Tests ,Serum samples ,Enzymes ,Certified reference materials ,Chemistry, Clinical ,Regression Analysis ,Measurement uncertainty - Abstract
Background The metrological traceability of values for the catalytic concentration of several enzymes assigned to a calibration material has been assured by following the recently published International Standard ISO 18153. Methods A traceable value with a measurement uncertainty was assigned for the catalytic concentration of alanine aminotransferase, creatine kinase, gamma-glutamyltransferase and lactate dehydrogenase in two materials from different sources. These are all measurable quantities, with the primary reference measurement procedure described by the International Federation of Clinical Chemistry and Laboratory Medicine (IFCC) and a primary calibrator giving metrological traceability to the SI unit of measurement. The metrologically traceable calibration was validated by measuring human serum samples using the primary reference measurement procedure and a routine commercial measurement procedure calibrated with the traceable materials. Results Results showed that the primary reference procedure, selected manufacturers' procedures and the end-user's routine procedure for each enzyme have the same analytical specificity. Four of eight commercial calibrators tested were commutable, whereas the others had a very small difference in absolute terms, indicating that these materials would be useful for calibration. Conclusion The implementation of a reference system for enzyme measurements was demonstrated that assures the traceability of patient results to SI units.
- Published
- 2006
- Full Text
- View/download PDF
19. IFCC primary reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C. International Federation of Clinical Chemistry and Laboratory Medicine. Part 5. Reference procedure for the measurement of catalytic concentration of aspartate aminotransferase
- Author
-
Gerhard, Schumann, Roberto, Bonora, Ferruccio, Ceriotti, Georges, Férard, Carlo A, Ferrero, Paul F H, Franck, F Javier, Gella, Wieland, Hoelzel, Poul Jørgen, Jørgensen, Takashi, Kanno, Art, Kessner, Rainer, Klauke, Nina, Kristiansen, Jean-Marc, Lessinger, Thomas P J, Linsinger, Hideo, Misaki, Mauro, Panteghini, Jean, Pauwels, Françoise, Schiele, Heinz G, Schimmel, Gerhard, Weidemann, and Lothar, Siekmann
- Subjects
Solutions ,Kinetics ,Reference Values ,Humans ,Indicators and Reagents ,Aspartate Aminotransferases ,Clinical Enzyme Tests ,Hydrogen-Ion Concentration ,Catalysis - Abstract
This paper is the fifth in a series dealing with reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C and the certification of reference preparations. Other parts deal with: Part 1. The Concept of Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes; Part 2. Reference Procedure for the Measurement of Catalytic Concentration of Creatine Kinase; Part 3. Reference Procedure for the Measurement of Catalytic Concentration of Lactate Dehydrogenase; Part 4. Reference Procedure for the Measurement of Catalytic Concentration of Alanine Aminotransferase; Part 6. Reference Procedure for the Measurement of Catalytic Concentration of Gamma-Glutamyltransferase; Part 7. Certification of Four Reference Materials for the Determination of Enzymatic Activity of Gamma-Glutamyltransferase, Lactate Dehydrogenase, Alanine Aminotransferase and Creatine Kinase at 37 degrees C. A document describing the determination of preliminary upper reference limits is also in preparation. The procedure described here is deduced from the previously described 30 degrees C IFCC reference method. Differences are tabulated and commented on in Appendix 3.
- Published
- 2002
20. IFCC primary reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C. International Federation of Clinical Chemistry and Laboratory Medicine. Part 4. Reference procedure for the measurement of catalytic concentration of alanine aminotransferase
- Author
-
Gerhard, Schumann, Roberto, Bonora, Ferruccio, Ceriotti, Georges, Férard, Carlo A, Ferrero, Paul F H, Franck, F Javier, Gella, Wieland, Hoelzel, Poul Jørgen, Jørgensen, Takashi, Kanno, Art, Kessner, Rainer, Klauke, Nina, Kristiansen, Jean-Marc, Lessinger, Thomas P J, Linsinger, Hideo, Misaki, Mauro, Panteghini, Jean, Pauwels, Françoise, Schiele, Heinz G, Schimmel, Gerhard, Weidemann, and Lothar, Siekmann
- Subjects
Solutions ,Kinetics ,Reference Values ,Humans ,Alanine Transaminase ,Clinical Enzyme Tests ,Hydrogen-Ion Concentration ,Catalysis - Abstract
This paper is the fourth in a series dealing with reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C and the certification of reference preparations. Other parts deal with: Part 1. The Concept of Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes; Part 2. Reference Procedure for the Measurement of Catalytic Concentration of Creatine Kinase; Part 3. Reference Procedure for the Measurement of Catalytic Concentration of Lactate Dehydrogenase; Part 5. Reference Procedure for the Measurement of Catalytic Concentration of Aspartate Aminotransferase; Part 6. Reference Procedure for the Measurement of Catalytic Concentration of Gamma-Glutamyltransferase; Part 7. Certification of Four Reference Materials for the Determination of Enzymatic Activity of Gamma-Glutamyltransferase, Lactate Dehydrogenase, Alanine Aminotransferase and Creatine Kinase at 37 degrees C. A document describing the determination of preliminary upper reference limits is also in preparation. The procedure described here is deduced from the previously described 30 degrees C IFCC reference method. Differences are tabulated and commented on in Appendix 2.
- Published
- 2002
21. IFCC primary reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C. International Federation of Clinical Chemistry and Laboratory Medicine. Part 7. Certification of four reference materials for the determination of enzymatic activity of gamma-glutamyltransferase, lactate dehydrogenase, alanine aminotransferase and creatine kinase accord
- Author
-
Lothar, Siekmann, Roberto, Bonora, Carl A, Burtis, Ferruccio, Ceriotti, Pascale, Clerc-Renaud, Georges, Férard, Carlo A, Ferrero, Jean-Claude, Forest, Paul F H, Franck, F-Javier, Gella, Wieland, Hoelzel, Poul Jørgen, Jørgensen, Takashi, Kanno, Art, Kessner, Rainer, Klauke, Nina, Kristiansen, Jean-Marc, Lessinger, Thomas P J, Linsinger, Hideo, Misaki, Mathias M, Mueller, Mauro, Panteghini, Jean, Pauwels, Françoise, Schiele, Heinz G, Schimmel, Arlette, Vialle, Gerhard, Weidemann, and Gerhard, Schumann
- Subjects
Quality Control ,L-Lactate Dehydrogenase ,Humans ,Reproducibility of Results ,Alanine Transaminase ,Guidelines as Topic ,gamma-Glutamyltransferase ,Clinical Enzyme Tests ,Reference Standards ,Creatine Kinase ,Enzymes - Abstract
This paper is the seventh in a series dealing with reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C and the certification of reference preparations. Other parts deal with: Part 1. The Concept of Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes; Part 2. Reference Procedure for the Measurement of Catalytic Concentration of Creatine Kinase; Part 3. Reference Procedure for the Measurement of Catalytic Concentration of Lactate Dehydrogenase; Part 4. Reference Procedure for the Measurement of Catalytic Concentration of Alanine Aminotransferase; Part 5. Reference Procedure for the Measurement of Catalytic Concentration of Aspartate Aminotransferase; Part 6. Reference Procedure for the Measurement of Catalytic Concentration of Gamma-Glutamyltransferase. A document describing the determination of preliminary reference values is also in preparation. The certification of the catalytic activity concentrations as determined by the recently elaborated IFCC primary reference methods at 37 degrees C of four enzyme preparations, namely IRMM/IFCC 452 (gamma-glutamyltransferase), IRMM/IFCC 453 (lactate dehydrogenase 1), IRMM/IFCC 454 (alanine aminotransferase) and IRMM/IFCC 455 (creatine kinase) is described. Homogeneity data were derived from previous results. Stability was assessed using recently obtained data as well as data from previous stability studies. The collaborative study for value assignment was performed under a strict quality control scheme to ensure traceability to the primary reference method. Uncertainty of the materials was assessed in compliance with the Guide to the Expression of Uncertainty in Measurement. The certified values obtained at 37 degrees C are 1.90 microkat/l +/- 0.04 microkat/l (114.1 U/l +/- 2.4 U/l), for gamma-glutamyltransferase, 8.37 microkat/l +/- 0.12 microkat/l (502 U/l +/- 7 U/l), for lactate dehydrogenase 1, 3.09 microkat/l +/- 0.07 microkat/l (186 U/l +/- 4 U/l), for alanine aminotransferase and 1.68 microkat/l +/- 0.07 microkat/l (101 U/l +/- 4 U/l), for creatine kinase. The materials are intended for internal quality control as well as for the evaluation of test systems as required by recent European Union legislation. Furthermore, the materials can be used to transfer accuracy from a reference method to a routine procedure provided the procedures exhibit the same analytical specificity and the certified materials are commutable.
- Published
- 2002
22. IFCC primary reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C. Part 2. Reference procedure for the measurement of catalytic concentration of creatine kinase
- Author
-
Hideo Misaki, Arlette Vialle, Carlo A. Ferrero, Rainer Klauker, Poul J. Jørgensen, Wieland Hoelzel, Mauro Panteghini, Takashi Kanno, Jean-Marc Lessinger, Gerhard Weidemann, Pascale Clerc-Renaud, Jean Pauwels, Thomas P. J. Linsinger, Gerhard Schumann, Georges Férard, Lothar Siekmann, R. Bonora, Ferruccio Ceriotti, Heinz Schimmel, Paul F H Franck, F. Javier Gella, Art Kessne, and N Kristiansen
- Subjects
chemistry.chemical_classification ,Chromatography ,Catalytic concentration ,Biochemistry (medical) ,Clinical Biochemistry ,General Medicine ,Hydrogen-Ion Concentration ,Reference Standards ,Clinical method ,Catalysis ,Body Temperature ,Enzymes ,chemistry.chemical_compound ,Kinetics ,Enzyme ,Biochemistry ,chemistry ,Reference values ,Lactate dehydrogenase ,Chemistry, Clinical ,Humans ,Thermodynamics ,Alanine aminotransferase ,Quantitative analysis (chemistry) - Abstract
This paper is the second in a series dealing with reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C and the certification of reference preparations. Other parts deal with: Part 1. The Concept of Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes; Part 3. Reference Procedure for the Measurement of Catalytic Concentration of Lactate Dehydrogenase; Part 4. Reference Procedure for the Measurement of Catalytic Concentration of Alanine Aminotransferase; Part 5. Reference Procedure for the Measurement of Catalytic Concentration of Aspartate Aminotransferase; Part 6. Reference Procedure for the Measurement of Catalytic Concentration of gamma-Glutamyltransferase; Part 7. Certification of Four Reference Materials for the Determination of Enzymatic Activity of gamma-Glutamyltransferase, Lactate Dehydrogenase, Alanine Aminotransferase and Creatine Kinase at 37 degrees C. A document describing the determination of preliminary reference values is also in preparation. The pro- described 30 degrees C IFCC reference method (1). Differences are tabulated and commented on in Appendix 3.
- Published
- 2002
23. IFCC Primary Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes at 37°C. Part 4. Reference Procedure for the Measurement of Catalytic Concentration of Alanine Aminotransferase
- Author
-
Art Kessner, Georges Férard, Ferruccio Ceriotti, Hideo Misaki, Paul F H Franck, Françoise Schiele, Mauro Panteghini, Jean Pauwels, Rainer Klauke, Carlo A. Ferrero, Lothar Siekmann, Gerhard Weidemann, F. Javier Gella, Gerhard Schumann, Poul J. Jørgensen, Jean-Marc Lessinger, Takashi Kanno, N Kristiansen, Thomas P. J. Linsinger, Wieland Hoelzel, R. Bonora, and Heinz Schimmel
- Subjects
chemistry.chemical_classification ,Chromatography ,biology ,Chemistry ,Catalytic concentration ,Biochemistry (medical) ,Clinical Biochemistry ,L-Lactate dehydrogenase ,General Medicine ,Catalysis ,chemistry.chemical_compound ,Enzyme ,Biochemistry ,Reference values ,Lactate dehydrogenase ,biology.protein ,Creatine kinase ,Alanine aminotransferase - Abstract
This paper is the fourth in a series dealing with reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C and the certification of reference preparations. Other parts deal with: Part 1. The Concept of Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes; Part 2. Reference Procedure for the Measurement of Catalytic Concentration of Creatine Kinase; Part 3. Reference Procedure for the Measurement of Catalytic Concentration of Lactate Dehydrogenase; Part 5. Reference Procedure for the Measurement of Catalytic Concentration of Aspartate Aminotransferase; Part 6. Reference Procedure for the Measurement of Catalytic Concentration of Gamma-Glutamyltransferase; Part 7. Certification of Four Reference Materials for the Determination of Enzymatic Activity of Gamma-Glutamyltransferase, Lactate Dehydrogenase, Alanine Aminotransferase and Creatine Kinase at 37 degrees C. A document describing the determination of preliminary upper reference limits is also in preparation. The procedure described here is deduced from the previously described 30 degrees C IFCC reference method. Differences are tabulated and commented on in Appendix 2.
- Published
- 2002
- Full Text
- View/download PDF
24. IFCC Primary Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes at 37°C. Part 7. Certification of Four Reference Materials for the Determination of Enzymatic Activity of γ-Glutamyltransferase, Lactate Dehydrogenase, Alanine Aminotransferase and Creatine Kinase according to IFCC Reference Procedures at 37°C
- Author
-
Art Kessner, F-Javier Gella, Georges Férard, Paul F H Franck, Jean Pauwels, Mathias M. Mueller, Françoise Schiele, Rainer Klauke, Gerhard Schumann, Mauro Panteghini, Ferruccio Ceriotti, Gerhard Weidemann, Takashi Kanno, Carlo A. Ferrero, Jean-Claude Forest, Carl A Burtis, Lothar Siekmann, Arlette Vialle, N Kristiansen, Pascale Clerc-Renaud, R. Bonora, Heinz Schimmel, Hideo Misaki, Poul J. Jørgensen, Jean-Marc Lessinger, Wieland Hoelzel, and Thomas P. J. Linsinger
- Subjects
chemistry.chemical_classification ,Chromatography ,biology ,Biochemistry (medical) ,Clinical Biochemistry ,General Medicine ,Catalysis ,Internal quality ,chemistry.chemical_compound ,Enzyme ,Biochemistry ,chemistry ,Lactate dehydrogenase ,biology.protein ,media_common.cataloged_instance ,Creatine kinase ,Alanine aminotransferase ,Gamma-glutamyltransferase ,European union ,media_common - Abstract
This paper is the seventh in a series dealing with reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C and the certification of reference preparations. Other parts deal with: Part 1. The Concept of Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes; Part 2. Reference Procedure for the Measurement of Catalytic Concentration of Creatine Kinase; Part 3. Reference Procedure for the Measurement of Catalytic Concentration of Lactate Dehydrogenase; Part 4. Reference Procedure for the Measurement of Catalytic Concentration of Alanine Aminotransferase; Part 5. Reference Procedure for the Measurement of Catalytic Concentration of Aspartate Aminotransferase; Part 6. Reference Procedure for the Measurement of Catalytic Concentration of Gamma-Glutamyltransferase. A document describing the determination of preliminary reference values is also in preparation. The certification of the catalytic activity concentrations as determined by the recently elaborated IFCC primary reference methods at 37 degrees C of four enzyme preparations, namely IRMM/IFCC 452 (gamma-glutamyltransferase), IRMM/IFCC 453 (lactate dehydrogenase 1), IRMM/IFCC 454 (alanine aminotransferase) and IRMM/IFCC 455 (creatine kinase) is described. Homogeneity data were derived from previous results. Stability was assessed using recently obtained data as well as data from previous stability studies. The collaborative study for value assignment was performed under a strict quality control scheme to ensure traceability to the primary reference method. Uncertainty of the materials was assessed in compliance with the Guide to the Expression of Uncertainty in Measurement. The certified values obtained at 37 degrees C are 1.90 microkat/l +/- 0.04 microkat/l (114.1 U/l +/- 2.4 U/l), for gamma-glutamyltransferase, 8.37 microkat/l +/- 0.12 microkat/l (502 U/l +/- 7 U/l), for lactate dehydrogenase 1, 3.09 microkat/l +/- 0.07 microkat/l (186 U/l +/- 4 U/l), for alanine aminotransferase and 1.68 microkat/l +/- 0.07 microkat/l (101 U/l +/- 4 U/l), for creatine kinase. The materials are intended for internal quality control as well as for the evaluation of test systems as required by recent European Union legislation. Furthermore, the materials can be used to transfer accuracy from a reference method to a routine procedure provided the procedures exhibit the same analytical specificity and the certified materials are commutable.
- Published
- 2002
- Full Text
- View/download PDF
25. IFCC Primary Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes at 37C. Part 6. Reference Procedure for the Measurement of Catalytic Concentration of γ-Glutamyltransferase
- Author
-
Georges Férard, T Kanno, A Kessner, Jean Pauwels, R. Bonora, Heinz Schimmel, Jean-Marc Lessinger, Françoise Schiele, N Kristiansen, Rainer Klauke, F-Javier Gella, Wieland Hoelzel, Mauro Panteghini, Ferruccio Ceriotti, Thomas P. J. Linsinger, Gerhard Schumann, Hideo Misaki, Paul F H Franck, Carlo A. Ferrero, and Poul J. Jørgensen
- Subjects
chemistry.chemical_classification ,Primary (chemistry) ,Enzyme ,Chemistry ,Catalytic concentration ,Biochemistry (medical) ,Clinical Biochemistry ,Organic chemistry ,General Medicine ,Catalysis - Published
- 2002
- Full Text
- View/download PDF
26. IFCC Primary Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes at 37°C. Part 3. Reference Procedure for the Measurement of Catalytic Concentration of Lactate Dehydrogenase
- Author
-
T Kanno, Ferruccio Ceriotti, Poul J. Jørgensen, Jean Pauwels, F-Javier Gella, Mauro Panteghini, Carlo A. Ferrero, Gerhard Weidemann, Hideo Misaki, Paul F H Franck, Jean-Marc Lessinger, R. Bonora, Gerhard Schumann, Heinz Schimmel, A Kessner, Rainer Klauke, Lothar Siekmann, Georges Férard, N Kristiansen, Wieland Hoelzel, Thomas P. J. Linsinger, Pascale Clerc-Renaud, and Arlette Vialle
- Subjects
Quality Control ,chemistry.chemical_classification ,Chromatography ,biology ,Catalytic concentration ,Biochemistry (medical) ,Clinical Biochemistry ,General Medicine ,Hydrogen-Ion Concentration ,Reference Standards ,Body Temperature ,Enzymes ,Catalysis ,Kinetics ,chemistry.chemical_compound ,Enzyme ,chemistry ,Chemistry, Clinical ,Lactate dehydrogenase ,biology.protein ,Humans ,Thermodynamics ,Creatine kinase ,Alanine aminotransferase ,Reference standards - Abstract
This paper is the third in a series dealing with reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C and the certification of reference preparations. Other parts deal with: Part 1. The Concept of Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes; Part 2. Reference Procedure for the Measurement of Catalytic Concentration of Creatine Kinase; Part 4. Reference Procedure for the Measurement of Catalytic Concentration of Alanine Aminotransferase; Part 5. Reference Procedure for the Measurement of Catalytic Concentration of Aspartate Aminotransferase; Part 6. Reference Procedure for the Measurement of Catalytic Concentration of gamma-Glutamyltransferase; Part 7. Certification of Four Reference Materials tamyltransferase, Lactate Dehydrogenase, Alanine Aminotransferase and Creatine Kinase at 37 degrees C. A document describing the determination of preliminary upper reference limits is also in preparation. The procedure described here is deduced from the previously described 30 degrees C IFCC reference method (1). Differences are tabulated and commented on in Appendix 1.
- Published
- 2002
- Full Text
- View/download PDF
27. IFCC Primary Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes at 37°C. Part 1. The Concept of Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes
- Author
-
Takashi Kanno, Arlette Vialle, Ferruccio Ceriotti, R. Bonora, Heinz Schimmel, Hideo Misaki, Lothar Siekmann, Mauro Panteghini, N Kristiansen, Thomas P. J. Linsinger, Françoise Schiele, Georges Férard, Carlo A. Ferrero, Poul J. Jørgensen, Rainer Klauke, Jean Claude Forest, Art Kessner, Paul F H Franck, Pascale Clerc-Renaud, Jean Pauwels, Carl A Burtis, Wieland Hoelzel, Mathias M. Mueller, Gerhard Weidemann, Jean Marc Lessinger, Gerhard Schumann, and F. Javier Gella
- Subjects
Quality Assurance, Health Care ,Catalytic concentration ,Clinical Biochemistry ,Catalysis ,chemistry.chemical_compound ,Lactate dehydrogenase ,Humans ,Alanine aminotransferase ,chemistry.chemical_classification ,Primary (chemistry) ,biology ,Chemistry ,Biochemistry (medical) ,Temperature ,Reproducibility of Results ,General Medicine ,Hydrogen-Ion Concentration ,Reference Standards ,Enzymes ,Kinetics ,Enzyme ,Biochemistry ,Chemistry, Clinical ,Reference values ,biology.protein ,Thermodynamics ,Creatine kinase - Abstract
This paper is the first in a series dealing with reference procedures for the measurement of catalytic activity concentrations of enzymes at 37 degrees C and with the certification of reference preparations. Other parts deal with: Part 2. Reference Procedure for the Measurement of Catalytic Concentration of Creatine Kinase; Part 3. Reference Procedure for the Measurement of Catalytic Concentration of Lactate Dehydrogenase; Part 4. Reference Procedure for the Measurement of Catalytic Concentration of Alanine Aminotransferase; Part 5. Reference Procedure for the Measurement of Catalytic Concentration of Aspartate Aminotransferase; Part 6. Reference Procedure for the Measurement of Catalytic fication of Four Reference Materials for the Determination of Enzymatic Activity of y-Glutamyltransferase, Lactate Dehydrogenase, Alanine Aminotransferase and Creatine Kinase at 37 degrees C. A document describing the determination of preliminary reference values is also in preparation.
- Published
- 2002
- Full Text
- View/download PDF
28. Creatine kinase 2 mass measurement: methods comparison and study of the matrix effect
- Author
-
Teresa Palencia, Francesca Canalias, F. Javier Gella, and Maribel Sánchez
- Subjects
Immunoassay ,medicine.medical_specialty ,Chromatography ,biology ,business.industry ,Biochemistry (medical) ,Clinical Biochemistry ,General Medicine ,Biochemistry ,Mass measurement ,Endocrinology ,Method comparison ,Human plasma ,Internal medicine ,Intermethod comparison ,Calibration ,Creatine kinase isoenzyme ,biology.protein ,Medicine ,Humans ,Creatine kinase ,CK - Creatine kinase ,business ,Quantitative analysis (chemistry) ,Creatine Kinase - Abstract
Five different commercial immunoassays for the measurement of creatine kinase isoenzyme 2 mass concentration were compared using human plasma samples covering a wide range of creatine kinase 2 concentrations. The immunoassays studied differ in the detection systems, in the specificity of the antibodies and in the calibrators used. Intermethod comparison by regression analysis showed differences in the results of creatine kinase 2 mass concentration. The following ratios were deduced from the obtained equations: Elecsys=1.10×Immulite=1.20×IMx=1.26×ACS:180=1.33×Stratus. The commutability of different materials prepared by diluting purified human creatine kinase 2 in biological and synthetic matrices was studied using the different immunoassays in comparison with human plasma specimens. Almost all the materials tested were not commutable.
- Published
- 1999
29. Calibration and traceability of enzyme and antibody measurements
- Author
-
Francesca Canalias and F-Javier Gella
- Subjects
Measurement method ,Traceability ,Standardization ,Computer science ,Stereochemistry ,Biochemistry (medical) ,Clinical Biochemistry ,General Medicine ,computer.software_genre ,Biochemistry ,Antibodies ,Catalysis ,Enzymes ,Reference Values ,Calibration ,Humans ,Data mining ,computer - Published
- 1999
30. Production and certification of an enzyme reference material for creatine kinase isoenzyme 2 (CRM 608)
- Author
-
Donald W. Moss, Amparo Galán, Françoise Schiele, Elena Frey, Klaus Lorentz, Francesca Canalias, F. Javier Gella, Mogens Hørder, Ferruccio Ceriotti, and Anthony G. Hadjivassiliou
- Subjects
Sodium ,Clinical Biochemistry ,chemistry.chemical_element ,Biochemistry ,Catalysis ,Reference Values ,Enzyme Stability ,medicine ,Humans ,Enzyme activity ,Polyacrylamide gel electrophoresis ,Creatine Kinase ,Ethanol precipitation ,chemistry.chemical_classification ,Chromatography ,biology ,Myocardium ,Biochemistry (medical) ,General Medicine ,Human serum albumin ,Chromatography, Ion Exchange ,Enzyme assay ,Isoenzymes ,Kinetics ,Isoelectric point ,Enzyme ,Freeze Drying ,chemistry ,biology.protein ,Creatine kinase ,Electrophoresis, Polyacrylamide Gel ,Reference material ,Standardisation ,medicine.drug - Abstract
We describe the preparation of a lyophilized material containing purified human creatine kinase 2 (CK-MB), and the certification of its catalytic concentration. The material can be used to verify the comparability of results from different laboratories, for intra-laboratory quality control, or for calibration of the creatine kinase 2 catalytic concentration measurements. The enzyme was purified from human heart by ethanol precipitation and chromatography successively on DEAE-Sephacel and Blue-Sepharose. The purified enzyme had a specific activity of 998.4 U/mg and was >99% pure on polyacrylamide gel electrophoresis. The material was examined for several possible contaminating enzymes, which were found to be absent. The purified creatine kinase 2 had two subunits (B and M) with molecular masses of 43 650 and 41 700 g/mol, respectively, and an isoelectric point at pH 5.8. The material was prepared by diluting the purified creatine kinase 2 in a matrix containing 25 mmol/L PIPES buffer, pH 7.2, 2 mmol/L ADP, 5 mmol/L 2-mercaptoethanol, 154 mmol/L sodium chloride and 50 g/L human serum albumin, dispensing it into vials and freeze-drying. The batch was shown to be homogeneous. The loss of enzyme activity on storage at -20°C is predicted to be less than 0.18% per annum on the basis of accelerated degradation studies. The catalytic concentration of creatine kinase in samples of the reconstituted material is certified to be 67.2±1.8 U/L (1.12±0.03 μkat/L) when measured, at 30°C, by the Recommended Method of the International Federation of Clinical Chemistry. Copyright (C) 1998 Elsevier Science B.V.
- Published
- 1998
- Full Text
- View/download PDF
31. Determination of total and pancreatic alpha-amylase in human serum with 2-chloro-4-nitrophenyl-alpha-D-maltotrioside as substrate
- Author
-
Francesca Canalias, F. Javier Gella, Gemma Gubern, and Ricardo Vidal
- Subjects
Stereochemistry ,Sodium ,Clinical Biochemistry ,chemistry.chemical_element ,Calcium ,Buffers ,Sodium Chloride ,Biochemistry ,Sensitivity and Specificity ,Nitrophenols ,chemistry.chemical_compound ,Calcium Chloride ,Potassium thiocyanate ,Humans ,Amylase ,Saliva ,Pancreas ,Chromatography ,biology ,Spectrophotometry, Atomic ,Biochemistry (medical) ,Temperature ,Substrate (chemistry) ,General Medicine ,Hydrogen-Ion Concentration ,chemistry ,Reagent ,biology.protein ,Ethanesulfonic acid ,Hemoglobin ,alpha-Amylases ,Trisaccharides - Abstract
A reagent and assay conditions for the determination of the catalytic concentration of alpha-amylase (E.C. 3.2.1.1) in serum with 2-chloro-4-nitrophenyl-alpha-D-maltotrioside as substrate are described. The selected reaction mixture contains 50 mmol/l 2-(N-morpholino)ethanesulfonic acid buffer at pH 6.1 (37 degrees C), 300 mmol/l sodium chloride, 5 mmol/l calcium chloride and 450 mmol/l potassium thiocyanate. The described method is suitable for the measurement of total as well as pancreatic alpha-amylase by including antibodies against the salivary isoenzyme. The method shows the absence of a lag phase period, is sensitive and precise, has a large analytical range and is free from interference by hemoglobin, bilirubin and triglycerides. Comparative studies showed good correlation with other well established methods.
- Published
- 1997
32. Study of the Stability of Creatine Kinase in Control Materials
- Author
-
Yolanda Saco, F. Javier Gella, and Francesca Canalias
- Subjects
Quality Control ,Chromatography ,Catalytic concentration ,Biochemistry (medical) ,Clinical Biochemistry ,education ,Temperature ,General Medicine ,Reference Standards ,Biology ,Biochemistry ,Chemistry, Clinical ,Enzyme Stability ,biology.protein ,Humans ,Creatine kinase ,Reagent Kits, Diagnostic ,Creatine Kinase ,Reference standards - Abstract
We examined the stability of twelve control materials from different suppliers containing creatine kinase. The stability was assessed storing preparations at 4 degrees C, 27 degrees C and 37 degrees C and periodically measuring creatine kinase catalytic concentration. The activity was significantly greater when the lyophilized material was reconstituted with water at 4 degrees C as compared to 27 degrees C and 37 degrees C. All preparations tested showed good stability at 4 degrees C over a 72 hour period. We considered the suitability of tested control materials for quality-control purposes.
- Published
- 1995
33. Purification and characterization of streptolysin O from Streptococcus pyogenes
- Author
-
Jorge Beleta, Jordi Viver, Francesc Gonzalez-Sastre, Francesca Canalias, and F. Javier Gella
- Subjects
Streptococcus pyogenes ,Ion chromatography ,Polyethylene glycol ,Tetanus Antitoxin ,medicine.disease_cause ,Biochemistry ,chemistry.chemical_compound ,Bacterial Proteins ,medicine ,Chromatography ,Molecular mass ,biology ,Temperature ,Reproducibility of Results ,Hydrogen-Ion Concentration ,Streptococcaceae ,biology.organism_classification ,Isoelectric point ,chemistry ,Streptolysins ,Erythrocyte Count ,Streptolysin ,Electrophoresis, Polyacrylamide Gel ,Isoelectric Focusing ,Exotoxin - Abstract
1. 1. Streptolysin O, an exotoxin produced by group A β-hemolytic streptococci, has been purified from Streptococcus pyogenes culture supernatants. 2. 2. The isolation and purification procedure involved ammonium sulphate and polyethylene glycol precipitations, and ion-exchange chromatographies on CM-Sepharose and Mono Q. 3. 3. The proposed procedure introduces two ion-exchange chromatography steps making the purification process simpler and, especially, more reproducible than other described protocols. 4. 4. The purified Streptolysin O was hemolytically active, had a specific activity of 415,000 HU/mg, an optimum pH of 7.0, a relative molecular mass of 60,100 and an isoelectric pH of 7.5.
- Published
- 1992
34. A simple procedure for the routine determination of aspartate aminotransferase and alanine aminotransferase with pyridoxal phosphate
- Author
-
F. Javier Gella, Rosendo Moreno, J.Antonio Gomez, Joaquin Arenas, M.Cruz Pastor, Teresa Olivella, and Rafael Durban
- Subjects
Erythrocytes ,biology ,Biochemistry (medical) ,Clinical Biochemistry ,Alanine Transaminase ,General Medicine ,Biochemistry ,Catalysis ,Cofactor ,chemistry.chemical_compound ,chemistry ,Pyridoxal Phosphate ,Reagent ,Pyruvic Acid ,biology.protein ,Humans ,Citrate synthase ,Indicators and Reagents ,Aspartate Aminotransferases ,Pyruvic acid ,Alanine aminotransferase ,Pyridoxal phosphate ,Pyruvates - Abstract
The preferred techniques for determination of the catalytic activity of aspartate aminotransferase (AST; EC 2.6.1.2) are those first described by Karmen, Wroblewski and La Due [1,2] and later improved by several Societies of Clinical Chemistry [3-51, in which oxaloacetate or pyruvate formed are enzymatically reduced to malate or lactate with concomitant oxidation of NADH. More recently, it has been found that serum aminotransferases may be undersaturated with the coenzyme pyridoxal phosphate [6-Q which should be included in the reaction mixture to improve the accuracy and the diagnostic sensitivity of the aminotransferases determination. The proposed IFCC methods for AST [9,10] and ALT [ll] saturate serum aminotransferases with pyridoxal phosphate during a lo-mm period of preincubation and the reaction is then initiated by addition of 2-oxoglutarate. The IFCC recommendations, that can be considered ‘reference methods’ [12], are inappropriate for use as routine methods in many laboratories because the use of two reagents and the long preincubation period of 10 min are serious inconveniences. We have studied a modification of the IFCC methods for AST and ALT that simplifies the procedure. The proposed procedure can use commercially available reagent kits and can be easily mechanised.
- Published
- 1985
- Full Text
- View/download PDF
35. Assay of glutaminase activity by colorimetric determination of glutamate
- Author
-
M. Angeles Pascual and F. Javier Gella
- Subjects
Biophysics ,Tetrazolium Salts ,Biology ,Kidney ,Biochemistry ,Glutaminase activity ,chemistry.chemical_compound ,Glutamate Dehydrogenase ,Glutamates ,Glutaminase ,Iodonitrotetrazolium ,Animals ,Molecular Biology ,chemistry.chemical_classification ,Chromatography ,Glutamate dehydrogenase ,Glutamate receptor ,Cell Biology ,Hydrogen-Ion Concentration ,Glutamine ,Enzyme ,chemistry ,Methylphenazonium Methosulfate ,Cattle ,Colorimetry ,Formazan - Abstract
An assay method for glutaminase is described in which the rate of release of glutamate from glutamine is followed in a second step by means of two coupled reactions involving glutamate dehydrogenase and the phenazine methosulfate-catalyzed reduction of iodonitrotetrazolium chloride by NADH. The assay is rapid, sensitive, and reproducible, and may be employed to determine glutaminase activity in crude as well as in purified enzyme preparations.
- Published
- 1982
- Full Text
- View/download PDF
36. Purification and characterization of two phosphorylase phosphatases from rabbit liver
- Author
-
Jorge Beleta, F. Javier Gella, and Pilar Benedicto
- Subjects
Macromolecular Substances ,Protein subunit ,Phosphatase ,Biochemistry ,Phosphates ,Glycogen phosphorylase ,Fluorides ,Adenosine Triphosphate ,medicine ,Phosphoprotein Phosphatases ,Animals ,Phosphorylase Phosphatase ,Tartrate-resistant acid phosphatase ,biology ,Molecular mass ,Acid phosphatase ,Trypsin ,Molecular biology ,Diphosphates ,Isoenzymes ,Molecular Weight ,(phosphorylase) phosphatase ,Liver ,biology.protein ,Rabbits ,medicine.drug - Abstract
Two phosphorylase phosphatase activities (I and III) have been purified from rabbit liver, with respective molecular weights of 117,000 and 230,000. Phosphatase III contained three different subunits of molecular weights 35,000, 67,000 and 80,000. Phosphatase I although majoritary in the preparation, was not homogeneous. Both phosphatases were dissociated by 2-mercaptoethanol treatment, releasing a catalytic subunit with a molecular weight of about 35,000. Phosphatases I and III activities responded very differently to incubation with trypsin and to ethanol precipitation. Phosphatase III was much more sensitive to inactivation by several ions and ATP than phosphatase I. On the basis of the obtained data, phosphatase I can be classified as a type-1 phosphatase and phosphatase III as a type-1 phosphatase.
- Published
- 1987
37. Lymphocyte phosphorylase kinase
- Author
-
Jorge Beleta, Enrique Concustell, and F. Javier Gella
- Subjects
Molar concentration ,Cations, Divalent ,Phosphorylase Kinase ,Swine ,Biology ,Biochemistry ,Chromatography, DEAE-Cellulose ,Glycogen phosphorylase ,Fluorides ,Adenosine Triphosphate ,Animals ,Magnesium ,Lymphocytes ,Phosphorylase kinase ,Protein kinase A ,Incubation ,chemistry.chemical_classification ,Kinase ,Hydrogen-Ion Concentration ,Molecular biology ,Enzyme assay ,Molecular Weight ,Enzyme ,chemistry ,biology.protein ,Chromatography, Gel - Abstract
1. 1. Phosphorylase kinase from pig lymphocytes has been purified 275-fold. 2. 2. The molecular weight of the purified enzyme was found to be 200,000. 3. 3. Optimum pH of the enzyme was dependent on ATP-Mg 2+ concentration. 4. 4. Maximum activity was obtained at equivalent molar concentration of ATP and Mg 2+ . 5. 5. Enzyme activity was partially dependent on Ca 2+ ions. 6. 6. K m of the kinase for substrates phosphorylase b and ATP were 8.7 μM and 0.1 mM, respectively. 7. 7. The activity of the purified enzyme was not affected by incubation with protein kinase, ATP and Mg 2+ .
- Published
- 1981
38. Study of the stability of creatine kinase in control materials.
- Author
-
Canalias F, Saco Y, and Javier Gella F
- Subjects
- Chemistry, Clinical standards, Enzyme Stability, Humans, Quality Control, Reagent Kits, Diagnostic, Reference Standards, Temperature, Creatine Kinase chemistry, Creatine Kinase metabolism
- Abstract
We examined the stability of twelve control materials from different suppliers containing creatine kinase. The stability was assessed storing preparations at 4 degrees C, 27 degrees C and 37 degrees C and periodically measuring creatine kinase catalytic concentration. The activity was significantly greater when the lyophilized material was reconstituted with water at 4 degrees C as compared to 27 degrees C and 37 degrees C. All preparations tested showed good stability at 4 degrees C over a 72 hour period. We considered the suitability of tested control materials for quality-control purposes.
- Published
- 1995
- Full Text
- View/download PDF
39. Purification and characterization of streptolysin O from Streptococcus pyogenes.
- Author
-
Canalias F, Viver J, Beleta J, Gonzalez-Sastre F, and Javier Gella F
- Subjects
- Bacterial Proteins, Electrophoresis, Polyacrylamide Gel, Erythrocyte Count, Hydrogen-Ion Concentration, Isoelectric Focusing, Reproducibility of Results, Streptolysins antagonists & inhibitors, Streptolysins chemistry, Temperature, Tetanus Antitoxin, Streptococcus pyogenes chemistry, Streptolysins isolation & purification
- Abstract
1. Streptolysin O, an exotoxin produced by group A beta-hemolytic streptococci, has been purified from Streptococcus pyogenes culture supernatants. 2. The isolation and purification procedure involved ammonium sulphate and polyethylene glycol precipitations, and ion-exchange chromatographies on CM-Sepharose and Mono Q. 3. The proposed procedure introduces two ion-exchange chromatography steps making the purification process simpler and, especially, more reproducible than other described protocols. 4. The purified streptolysin O was hemolytically active, had a specific activity of 415,000 HU/mg, an optimum pH of 7.0, a relative molecular mass of 60,100 and an isoelectric pH of 7.5.
- Published
- 1992
- Full Text
- View/download PDF
40. Lymphocyte phosphorylase kinase.
- Author
-
Javier Gella F, Beleta J, and Concustell E
- Subjects
- Adenosine Triphosphate metabolism, Animals, Cations, Divalent metabolism, Chromatography, DEAE-Cellulose, Chromatography, Gel, Fluorides pharmacology, Hydrogen-Ion Concentration, Magnesium pharmacology, Molecular Weight, Swine, Lymphocytes enzymology, Phosphorylase Kinase isolation & purification
- Published
- 1981
- Full Text
- View/download PDF
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.