18 results on '"J.P. Muh"'
Search Results
2. Characterization of N-glycosylated type I collagen in streptozotocin-induced diabetes
- Author
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J.P. Muh, A Le Pape, and A J Bailey
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Male ,Glycosylation ,Chemical Phenomena ,Lysine ,Mannose ,Borohydrides ,In Vitro Techniques ,Hydroxylysine ,Biochemistry ,Diabetes Mellitus, Experimental ,Tendons ,chemistry.chemical_compound ,Amadori rearrangement ,Animals ,Glycosides ,Molecular Biology ,Hexoses ,Rats, Inbred Strains ,Cell Biology ,Rats ,Chemistry ,chemistry ,Galactose ,O-linked glycosylation ,Collagen ,Oxidation-Reduction ,Type I collagen ,Research Article - Abstract
The N epsilon-glycosylation of lysine and hydroxylysine residues in collagen from streptozotocin-induced-diabetic rats was confirmed and the stability of the complex shown to be due to an Amadori rearrangement. The studies also demonstrate the relative specificities of glucose, galactose and mannose in their reaction with collagen. The glycosylation of lysine in vitro occurs with glucose and galactose, but not with mannose, whereas only gucose reacts with hydroxylysine to any significant extent. Glycosylation of collagen occurs slowly during normal aging, but in contrast with reports suggesting accelerated aging of collagen in diabetic animals, we clearly demonstrated that the apparent increased stability is not due to an acceleration of the normal maturation process involving the reducible cross-links.
- Published
- 1981
3. Interet des marqueurs cliniques et biologiques dans les syndromes autistiques de l'enfant
- Author
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Catherine Barthélémy, J.P. Muh, Bruneau N, Joëlle Martineau, B Garreau, and Lelord G
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Gynecology ,medicine.medical_specialty ,Physiology ,medicine ,Neurology (clinical) ,Psychology - Abstract
Resume Un certain nombre d'arguments plaident en faveur d'un dysfonctionnement des systemes monoaminergiques dans l'autisme de l'enfant. Des etudes utilisant des marqueurs cliniques, electrophysiologiques et biochimiques appuient notamment l'hypothese dopaminergique et seront exposees dans cette etude. Une analyse factorielle effectuee sur les notes obtenues a l'echelle clinique (« evaluation resumee du comportement autistique ) met en evidence un facteur I d'autisme correspondant aux criteres d'autisme du DSM III. Elle montre egalement que les troubles de l'attention et de la perception observes chez ces enfants appartiennent bien au facteur I. Ainsi, les perturbations de l'attention selective et de la perception de l'environment apparaissent comme des symptomes primaires des syndromes autistiques. Les enregistrements electrophysiologiques effectues chez les enfants autistiques montrent a la fois un trouble de la modulation des influx sensoriels et des anomalies de la capacite a associer deux stimulations de modalites sensorielles differentes. Ces donnees cliniques et electrophysiologiques peuvent etre reliees a l'hypothese dopaminergique. Les taux eleves de l'acide homovanillique, principal metabolite de la dopamine, observes chez certains enfants autistiques, traduisent egalement un trouble du metabolisme de la dopamine. Les relations trouvees entre ces differents marques sont discutees.
- Published
- 1987
4. Effects of in vitro N-glucosylation on type-I collagen fibrillogenesis
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A. Le Pape, J.D. Guitton, P. Y. Sizaret, and J.P. Muh
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Time Factors ,Chemistry ,Temperature ,Biophysics ,Fibrillogenesis ,macromolecular substances ,Cell Biology ,Fibril ,Biochemistry ,In vitro ,Rats ,law.invention ,Hydrophobic effect ,Microscopy, Electron ,Collagen, type I, alpha 1 ,Glucose ,Nephelometry and Turbidimetry ,law ,Animals ,Collagen ,Turbidimetry ,Electron microscope ,Molecular Biology ,Type I collagen - Abstract
Acid-soluble collagen from rat tail tendon was glucosylated in vitro and fibrillogenesis parameters were determined first at 35 degrees C then at 4 degrees C. Increased lag phase and half time were shown to be related to the amount of non-enzymatically bound glucose, probably due to a decrease of hydrophobic interactions at this early stage of fibril formation. The absence of intermolecular cross-links and the partial redissolution of fibrils of 4 degrees C, as investigated both by turbidimetry and electron microscopy, suggests a defect in the maturation process in glucosylated collagen fibrils.
- Published
- 1981
5. Contents, Vol. 3, 1980
- Author
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Jacques Chanard, Anton Szymanowicz, Kazuaki Yamada, Sarwan S. Kang, Eileen F. Smith, Gerard M. Turino, J. Rakotoarivony, Kenji Iesato, P.L. Oe, E. Maxa, Nishio Honda, J.M. Foidart, Jose R. Manaligod, G. D’Amico, A. Bellini, L.A.M. Stolte, P. Bardos, J.A. Velosa, Hans Jørgen G. Gundersen, Barbara A. McKenna, Farhad Khalil-Manesh, Wesley Fox, L. van Delden, M. Sternberg, G.J. Fleuren, W.A. Day, A.R. McGiven, L.H. Noel, L.O. Simpson, Tito Cavallo, Philippe Birembaut, Jean-Pierre Brunois, Dick Heinegård, Friedrich C. Luft, Thomas W. Huang, Paul D. Benya, Billy G. Hudson, S.-L. Ou, Ruth Østerby, Cristina Kenney, Eric Sanders, R.J. Winand, Raymond C. Duhamel, Arnold Pollak, J.H. Veerkamp, Kunio Okuda, K. Hempel, Edward C. Carlson, J. Yudkin, J.M. Suc, Rytter Nørgaard, J.R. Rüttner, Wilhelm Kriz, Sarah A. Taylor, Michael F. Bryson, Jared J. Grantham, Harro Buss, H.E. Abboud, J. Goldman, T. Heck, R.G. Spiro, G. Sperk, Peter Schneider, Godfrey Heathcote, J.C. Orfila, O.T. Uttendorfsky, Gareth J. Thomas, James L. Borke, Harold C. Slavkin, S.V. Shah, I. Molenaar, R. Habib, Paul Jacques Borel, W. Schurer, C.F. Lange, M. Levy, Rajinder P. Nayyar, Kelvin T. Hughes, D. Droz, E.C.M. Ooms, L.A.H. Monnens, G. Rauscher, Jörgen Wieslander, C. Dubois, N.W. Levin, H.U. Lange, G. Goffinet, Teruo Mori, Kjartan Seyer-Hansen, Michael E. Grant, K.H. Winterhalter, F. Dumler, Will W. Minuth, Earl P. Benditt, B.F. Odermatt, Masafumi Wakashin, Frederick I. Volini, Günter Hollweg, Richard D. Spall, P.R. Macdonald, Olivier Toupance, C. Dechenne, A.P. Evan, J.P.M. Langeveld, Eiich Matsuo, G. Lubec, Cecil A. Krakower, Barry S. Oemar, H. Takamiya, Rufino C. Pabico, Elias Meezan, S. Batsford, J. Leibowitch, Gerald A. Coles, P. Graaff, G. Simbruner, Gert Lubec, W. Romen, C. Naizot, Yasumasa Takaya, A. Pollak, Bonnie Anderson Bray, Shiro Ueda, G. Colasanti, A.P. Sahu, Ines Mandl, F.C. Luft, Malcolm Davies, Bernard J. Partner, P. Mahieu, A. Vogt, T.P. Dousa, Yoko Wakashin, J. Moran, Andrew P. Evan, P. Cortes, P.J. Hoedemaeker, Tadashi Ofuji, M. Spiess, J.B. Foidart, Sadia Muhammed, Per Gygren, Yoshio Mori, K.K. Venkatachalam, Mistumasa Nagase, Zensuke Ota, Izumi Takei, Y.S. Pirard, Ole Gøtzsche, B. Nabarra, J.P. Muh, E. Ratzenhofer, H. Coradello, Anne E. Jackson, Anna G. Brownell, Hirofumi Makino, O. Förster, P. Freychet, J.S. Hunt, M.C. Gubler, P.R. Mahieu, B.H. Spargo, Ralph J. Butkowski, E. Meezan, B. Trüeb, Klaus Brendel, T. Oite, and Robert G. Price
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Nephrology ,General Medicine ,Cardiology and Cardiovascular Medicine - Published
- 1980
6. Activités évoquées eeg (potentiels évoqués, ondes lentes) et troubles du métabolisme des acides aminés Chez Des Enfants Déficients Mentaux Profonds
- Author
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J.C. Arlot, Bruneau N, F. Laffont, I. Chevallier, J.P. Muh, Lelord G, and Jusseaume P
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chemistry.chemical_classification ,medicine.medical_specialty ,Physiology ,Hand anomalies ,Chemistry ,Mentally retarded ,Mentally deficient ,Amino acid ,Endocrinology ,Biochemistry ,Internal medicine ,medicine ,Neurology (clinical) ,Amino acid metabolism - Abstract
Summary This study proposes to show the possible relationships between, on the one hand, modifications of evoked potentials (E.P.) and slow potentials (S.P.) and, on the other hand anomalies in amino acid metabolism in mentally deficient children. Thirty-two mentally retarded children (I. Q.'s between 20 and 40) were examined and divided into two groups : R1 with no amino acid anomalies ; R2 with amino acid anomalies, « isolatedor associated with phosphocalcium metabolism perturbations or renal dysfunction. As predicted by previous observations, these mentally deficient children presented low amplitude E.P. and S.P. irrespective of their group assignment. Both pathological groups are characterised by a lack of E. P. conditioning. Moderate differences are observed between the two groups, R1 and R2. These differences are most evident in E.P. amplitude and less evident in S.P. These responses are weaker in group R2 than in R1. Within group R2 they are also weaker for those children with isolated amino acide anomalies. The low amplitude of evoked potentials observed in mentally retarded children can be linked, not only to perceptive and cognitive factors, but to biological factors.
- Published
- 1978
7. Purification and characterization of ubiquitin from mammalian testis
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J.P. Muh, Pierre Sautiere, Yves Menezo, Maurice Loir, A. Caraty, and M. Lanneau
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Male ,Gel filtration chromatography ,Chromosomal Proteins, Non-Histone ,Protein Conformation ,Size-exclusion chromatography ,Radioimmunoassay ,Biophysics ,Biology ,Biochemistry ,Protein structure ,Ubiquitin ,Structural Biology ,Testis ,Genetics ,Animals ,Amino Acid Sequence ,Amino Acids ,Ubiquitins ,Molecular Biology ,Peptide sequence ,Mammals ,chemistry.chemical_classification ,Mammalian testis ,Cell Biology ,Molecular biology ,Nucleoprotein ,Amino acid ,Nucleoproteins ,chemistry ,Chromatography, Gel ,biology.protein ,Oxidation-Reduction ,Amino acid analysis - Abstract
Ubiquitin was extracted from testis of 4 mammals and purified to homogeneity by gel filtration chromatography. Amino acid compositions and NH2-terminal sequences were found to be identical in the 4 species and with calf thymus ubiquitin. Ubiquitin conformation was shown to be very sensitive to oxidation. Improved methods for radioimmunoassay of ubiquitin in tissue extracts are also discussed.
- Published
- 1984
8. Isolation of two rat α-1-macroglobulin components by means of preparative isotachophoresis
- Author
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J.P. Muh, N. Gutman, F. Gauthier, and H. Mouray
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Electrophoresis ,Male ,Chromatography ,medicine.diagnostic_test ,Chemistry ,Biophysics ,Cell Biology ,Immunoelectrophoresis ,Biochemistry ,Rats ,Macroglobulin ,Molecular Weight ,Epitopes ,Sialic Acids ,medicine ,Animals ,alpha-Macroglobulins ,Isotachophoresis ,Molecular Biology - Abstract
A technique of preparative isotachophoresis is described for the preparation of two rat α-1-macroglobulin varieties. The procedure permits a good and fast separation. Antigenic identity of these components is shown by fused rocket immunoelectrophoresis. Some properties of the two varieties are determined, and causes of heterogeneity are also discussed.
- Published
- 1976
9. Modulation de l'amplitude des potentiels evoques auditifs en fonction de l'intensite de la stimulation. relation avec le metabolisme dopaminergique
- Author
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Catherine Barthélémy, J. Jouve, J.P. Muh, Bruneau N, and Lelord G
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medicine.medical_specialty ,chemistry.chemical_compound ,Endocrinology ,Physiology ,Chemistry ,Internal medicine ,Homovanillic acid ,Dopaminergic ,medicine ,Neurology (clinical) ,Dopamine metabolism - Abstract
Relationships between augmenting/reducing (aug/red) in auditory modality and dopaminergic metabolism were investigated in young normal adults. Auditory evoked potentials (AEP) to tones (750 Hz, 200 msec) varying from 50 to 80 sB SPL were recorded at Cz and Fz sites. Individual differences in dopaminergic metabolism were estimated by assaying homovanillic acid levels in urines (u-HVA). The slopes values of P1, N1 and P2 amplitude changes with increasing stimulus intensities were used to evaluate the relationships between aug/red and u-HVA levels. The results of this study showed significant negative correlations between the aug/red of the N1 component recorded at Fz site and the u-HVA concentrations: the higher the aug/red slopes (augmenting tendency), the lower the u-HVA levels. In fact, the main result was that this finding was in accordance with previous ones relating aug/red to HVA when assayed in cerebrospinal fluid (CSF). Our data also showed that in further studies on auditory aug/red, the interest should be focused on the N1 component at Fz site.
- Published
- 1987
10. Hypersensibilité immédiate au tétracosapeptide
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A. Sabbah, M.A. Garrigue, J.P. Muh, A. Sonneville, and J. Baudouin
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Anesthesiology and Pain Medicine ,Immunology and Allergy - Abstract
Resume Les auteurs rapportent une variete de cette allergie, particuliere, par le fait qu'il s'agit du Synacthene ordinaire et que le mode de reaction est un etat de mal asthmatique. Le diagnostic formel a ete porte sur la presence d'IgE specifiques au Synacthene pour l'un des malades. Apres une breve revue de la litterature, les auteurs emettent quelques hypotheses et discussions concernant le mecanisme intime de l'antigenicite.
- Published
- 1977
11. Isolation and Chemical Composition of Four Glycoproteins of the Renal Cortex of the Wistar Rat
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A. Tacquet, J.P. Muh, P. Bardos, and B. Devulder
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Electrophoresis ,Kidney Cortex ,Chemical Phenomena ,medicine.medical_treatment ,Renal cortex ,Kidney Glomerulus ,Basement Membrane ,Hydrolysate ,Cortex (anatomy) ,medicine ,Animals ,Trypsin ,Amino Acids ,Immunoelectrophoresis ,Saline ,Chemical composition ,Glycoproteins ,Hexoses ,chemistry.chemical_classification ,business.industry ,Immune Sera ,Glomerular basement membrane ,Hexosamines ,Chromatography, Ion Exchange ,Rats ,Chemistry ,medicine.anatomical_structure ,Biochemistry ,chemistry ,Chromatography, Gel ,Glycoprotein ,business ,medicine.drug - Abstract
Four crude glycoproteins were isolated from supernatant of a Wistar rat kidney cortex homogenate. Three were soluble in a saline solution at pH 7.5; a fourth was prepared from a trypsin hydrolysate. T
- Published
- 1974
12. Modifications of glomerular basement membrane cross-links in experimental diabetic rats
- Author
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Alain Le Pape, J.P. Muh, and J.D. Guitton
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Blood Glucose ,Male ,medicine.medical_specialty ,Glycosylation ,Kidney Glomerulus ,Biophysics ,Borohydrides ,Body weight ,Biochemistry ,Basement Membrane ,Diabetes Mellitus, Experimental ,chemistry.chemical_compound ,Internal medicine ,Diabetes mellitus ,medicine ,Animals ,Glycosides ,Amino Acids ,Molecular Biology ,Basement membrane ,chemistry.chemical_classification ,Glomerular basement membrane ,Body Weight ,Cell Biology ,medicine.disease ,Rats ,Amino acid ,medicine.anatomical_structure ,Endocrinology ,Membrane ,chemistry ,Urea ,Collagen - Abstract
Glomerular basement membranes were isolated from normal and streptozotocin-diabetic rats. after elimination of non collagenous components with 8M urea the extent of ketoamine-linked hexoses and cross-links in the preparation was determined using NaB 3 H 4 reduction and radiochromatography. The observed increase in the level of N-glycosylation appeared to be closely related to a lowered amount of intermolecular cross-links in diabetic rats as compared to normal animals. Such a glycosylation may affect the stability and physicochemical properties of G.B.M. and thereby contribute to the vascular sequelae of diabetes mellitus.
- Published
- 1981
13. Immunochemical study of some glycoproteins of the rat glomerular basement membrane
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P. Bardos, J.P. Muh, A. Tacquet, Luthier B, and B. Devulder
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Immunodiffusion ,Physiology ,Kidney Glomerulus ,Glycine ,Hydroxylysine ,Biochemistry ,Basement Membrane ,Hydrolysate ,Sepharose ,chemistry.chemical_compound ,medicine ,Animals ,Amino Acids ,Molecular Biology ,Fucose ,Glycoproteins ,Hexoses ,chemistry.chemical_classification ,Chromatography ,Glomerular basement membrane ,Hexosamines ,General Medicine ,Precipitin ,Glycopeptide ,Rats ,Hydroxyproline ,Microbial Collagenase ,medicine.anatomical_structure ,chemistry ,Sialic Acids ,Glycoprotein - Abstract
1. 1. The study of the amino acid composition, in particular the study of the hydroxyproline, hydroxylysine and glycine content, of the glycopeptide fractions obtained from a clostridropeptidase A hydrolysate of Wistar rat GBM allowed us to distinguish between two types of structure, one of which is collagen-like. 2. 2. Determination of carbohydrate composition revealed the existence of a heteropolysaccharidic glycane in all of the fractions studied. 3. 3. The study of the chemical composition of the high molecular weight components isolated using a Sepharose 4B column allowed us to distinguish between structural glycoproteins (Subfractions A 1 , A 2 , A 4 ) and collagen-like glycopeptides (Subfraction A 3 ) to which they are linked. 4. 4. The immunological studies revealed the antigenic complexity of the material studied and the existence of precipitin lines of identity for the fractions which were isolated.
- Published
- 1976
14. Distribution of non-enzymatically bound glucose in in vivo and in vitro glycosylated type I collagen molecules
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J.D. Guitton, Alain Le Pape, and J.P. Muh
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Male ,Glycosylation ,Biophysics ,Peptide ,Cleavage (embryo) ,Biochemistry ,chemistry.chemical_compound ,Structural Biology ,Glycation ,In vivo ,Genetics ,Animals ,Fluorometry ,Cyanogen Bromide ,Molecular Biology ,Fluorography ,chemistry.chemical_classification ,Chemistry ,Diabetes ,Nonenzymatic glycosylation ,Fibrillogenesis ,Rats, Inbred Strains ,Cell Biology ,In vitro ,Peptide Fragments ,Rats ,carbohydrates (lipids) ,Glucose ,CNBr cleavage ,Electrophoresis, Polyacrylamide Gel ,Collagen ,Glucose localization ,Type I collagen - Abstract
Non-enzymatic glycosylation of collagen occurs both in vivo during diabetes and in vitro after incubation with glucose. Glycosylated collagen exhibits altered physicochemical and biological properties which could explain some of the complications of diabetes. To provide a mechanistic explanation of this modification the localization of bound glucose was investigated using NaB[3H]H4 reduction and CNBr cleavage. Glucose fixation is distributed mainly on the alpha 1CB6 peptide after in vitro glycosylation whereas this distribution occurs less specifically during diabetes. It is concluded that fibrillogenesis alteration of in vitro glycosylated collagen is related to glucose fixation on free epsilon NH2 sites normally implied in intermolecular interactions.
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15. Mathematical studies of complement activation
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J.P. Muh, P. Bardos, and M.A. Garrigue
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Activator (genetics) ,Biochemistry (medical) ,Clinical Biochemistry ,Zymosan ,Complement Pathway, Alternative ,Inulin ,General Medicine ,Biochemistry ,Complement system ,chemistry.chemical_compound ,Classical complement pathway ,Kinetics ,chemistry ,Immunoglobulin M ,Immunoglobulin G ,Alternative complement pathway ,Humans ,Complement Pathway, Classical ,Complement Activation ,Mathematics - Abstract
Kinetic studies of complement activation were followed by hemolytic assay. Mathematical analysis shows that the curve is composed of two exponents: the first one, which occurs during a short span of time, represents the classical pathway, the second the alternative pathway. We were therefore able to foretell the respective participation of each activator used: inulin, zymosan, and aggregated immunoglobulins.
- Published
- 1983
16. Nonenzymatic glycosylation of collagen in diabetes: incidence on increased normal platelet aggregation
- Author
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A. Le Pape, N. Gutman, Yves Legrand, J.P. Muh, J.D. Guitton, and F. Fauvel
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Glycosylated collagen ,Male ,medicine.medical_specialty ,Platelet aggregation ,Platelet Aggregation ,Normal platelet aggregation ,Diabetes Mellitus, Experimental ,Glycation ,Physiology (medical) ,Internal medicine ,Diabetes mellitus ,medicine ,Animals ,Platelet ,Chemistry ,Incidence (epidemiology) ,Rats, Inbred Strains ,Thrombosis ,Hematology ,In vitro incubation ,medicine.disease ,Rats ,Endocrinology ,Glucose ,Biochemistry ,Collagen ,Protein Processing, Post-Translational - Abstract
The effect of normal and nonenzymatically glycosylated rat type I acid-soluble collagen on normal human platelets was investigated. Glycosylated collagen was obtained either after in vitro incubation with glucose or from rats made diabetic by streptozotocin. The amount of nonenzymatically bound glucose was as follows: normal 2.3, diabetic 7.6 and in vitro glycosylated collagen 9.0 nmol/mg. When investigated under conditions leading to identical diameters and molecular packings for all the samples, the aggregation potency was markedly stronger for diabetic and glycosylated collagens than for normal ones. These results show the potential role of this posttranslational modification of collagen which can be considered as a risk factor in the thrombotic pathogeny of diabetes.
- Published
- 1983
17. High-performance liquid chromatography with electrochemical detection for the simultaneous determination of the methoxylated amines, normetanephrine, metanephrine and 3-methoxytyramine, in urine
- Author
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N. Mariotte, J.P. Muh, J. Jouve, and C. Sureau
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Adult ,Male ,Adolescent ,Epinephrine ,Dopamine ,Urine ,Pheochromocytoma ,Normetanephrine ,Electrochemistry ,High-performance liquid chromatography ,chemistry.chemical_compound ,Chromatography detector ,Reference Values ,Humans ,Child ,Metanephrine ,Chromatography, High Pressure Liquid ,Chromatography ,Elution ,Extraction (chemistry) ,General Chemistry ,Middle Aged ,chemistry ,Child, Preschool ,Hypertension ,Female - Abstract
A simple method for the simultaneous analysis of normetanephrine, metanephrine and 3-methoxytyramine (both free and conjugated) in human urine by reversed-phase ion-pair high-performance liquid chromatography with electrochemical detection has been developed. Existing methods have been optimized for extraction by study of analytical parameters. The hydrolysed urines are purified and concentrated by successive passages on two ion-exchange resins and ammoniacal elution to eliminate interference from pigments or related chemical compounds. The methoxyamines are separated by high-performance liquid chromatography on a reversed-phase column. Detection and quantitation are achieved with an electrochemical detector using a vitreous carbon electrode. Samples can be injected at 25-min intervals. Reference values of adults and children are given.
- Published
- 1983
18. Influence of in vitro non-enzymatic glycosylation on the physicochemical parameters of type I collagen
- Author
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J.P. Muh, J.D. Guitton, and Alain Le Pape
- Subjects
Diphenylhexatriene ,Circular dichroism ,Protein Denaturation ,Glycosylation ,Hot Temperature ,Time Factors ,Chemical Phenomena ,Chemistry ,Isoelectric focusing ,Chemistry, Physical ,Viscosity ,Circular Dichroism ,In vitro ,Elasticity ,Rats ,chemistry.chemical_compound ,Electrophoresis ,Rheumatology ,Biochemistry ,Glycation ,Animals ,Collagen ,Isoelectric Focusing ,Type I collagen - Abstract
In vitro non-enzymatic condensation of glucose on acid soluble collagen is shown not to affect the molecular structure and stability as evaluated both by circular dichroism and differential spectrometry. Viscometric studies demonstrate a lowering in intermolecular interactions; whereas the hydrodynamic volume remains unaffected by nonenzymatic glycosylation. alpha 2(I) collagen chains exhibit a modified electrophoretic mobility previously found in collagen of diabetic rats; this peculiar behavior is discussed in terms of lowered hydrophobicity due to addition of hydrophilic groups from glucose. The lowered formation of hydrophobic areas, evaluated from the fluorescence emission of diphenylhexatriene, indicates that non-enzymatic glycosylation is able to influence the close packing of collagen fibers.
- Published
- 1984
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