15 results on '"McCormick WM"'
Search Results
2. Radiography of Atheromatous Disease Involving the Extracranial Arteries as Seen at Postmortem
- Author
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Stein, Bennett M., McCormick, Wm F., Rodriguez, Jesus N., and Taveras, Juan M.
- Published
- 1963
- Full Text
- View/download PDF
Catalog
3. THE ROENTGENOLOGY OF THE MENINGOHYPOPHYSEAL TRUNK
- Author
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PRIBRAM, H. F. W., primary, BOULTER, T. R., additional, and McCORMICK, WM. F., additional
- Published
- 1966
- Full Text
- View/download PDF
4. Untitled.
- Author
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McCORMICK, WM.
- Published
- 1856
5. Wapello Co., Iowa, Feb. 11, 1855.
- Author
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McCORMICK, WM.
- Published
- 1855
6. Horticulture.
- Author
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MCCORMICK, WM., P. A. E., J. N. F., HATHAWAY, A. H., and J. W.
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- 1872
7. An improved size exclusion-HPLC method for molecular size distribution analysis of immunoglobulin G using sodium perchlorate in the eluent.
- Author
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Wang H, Levi MS, Del Grosso AV, McCormick WM, and Bhattacharyya L
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- Adsorption, Chromatography, High Pressure Liquid methods, Immunoglobulin G chemistry, Perchlorates chemistry, Sodium Compounds chemistry
- Abstract
Size exclusion (SE) high performance liquid chromatography (HPLC) is widely used for the molecular size distribution (MSD) analyses of various therapeutic proteins. We report development and validation of a SE-HPLC method for MSD analyses of immunoglobulin G (IgG) in products using a TSKgel SuperSW3000 column and eluting it with 0.4M NaClO
4 , a chaotropic salt, in 40mM phosphate buffer, pH 6.8. The chromatograms show distinct peaks of aggregates, tetramer, and two dimers, as well as the monomer and fragment peaks. In addition, the method offers about half the run time (12min), better peak resolution, improved peak shape and more stable base-line compared to HPLC methods reported in the literature, including that in the European Pharmacopeia (EP). A comparison of MSD analysis results between our method and the EP method shows interactions between the protein and the stationary phase and partial adsorption of aggregates and tetramer on the stationary phase, when the latter method is used. Thus, the EP method shows lower percent of aggregates and tetramer than are actually present in the products. In view of the fact that aggregates have been attributed to playing a critical role in adverse reactions due to IgG products, our observation raises a major concern regarding the actual aggregate content in these products since the EP method is widely used for MSD analyses of IgG products. Our method eliminates (or substantially reduces) the interactions between the proteins and stationary phase as well as the adsorption of proteins onto the column. Our results also show that NaClO4 in the eluent is more effective in overcoming the protein/column interactions compared to Arg-HCl, another chaotropic salt. NaClO4 is shown not to affect the molecular size and relative distribution of different molecular forms of IgG. The method validated as per ICH Q2(R1) guideline using IgG products, shows good specificity, accuracy, precision and a linear concentration dependence of peak areas for different molecular forms. In summary, our method gives more reliable results than the SE-HPLC methods for MSD analyses of IgG reported in the literature, including the EP, particularly for aggregates and tetramer. The results are interpreted in terms of ionic (polar) and hydrophobic interactions between the stationary phase and the IgG protein., (Published by Elsevier B.V.) more...- Published
- 2017
- Full Text
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8. Protein Nitrogen Determination by Kjeldahl Digestion and Ion Chromatography.
- Author
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Wang H, Pampati N, McCormick WM, and Bhattacharyya L
- Subjects
- Animals, Cattle, Chromatography, Ion Exchange methods, Humans, Anthrax Vaccines analysis, Chemistry Techniques, Analytical methods, Nitrogen analysis, Ovalbumin analysis, Serum Albumin, Bovine analysis, Serum Albumin, Human analysis
- Abstract
We report development and validation of a simple, rapid, and accurate method for the quantitation of protein nitrogen, which combines Kjeldahl digestion and ion chromatography with suppressed conductivity detection and requires nanomolar amount of nitrogen in samples (≥10 μg protein). The mechanism of suppressed conductivity detection does not permit analysis of samples containing copper (present in Kjeldahl digestion solution) and aluminum (present in many vaccines as adjuvants) due to precipitation of their hydroxides within the suppressor. We overcame this problem by including 10 μM oxalic acid in Kjeldahl digests and in the eluent (30 mM methanesulfonic acid). The chromatography is performed using an IonPac CS-16 cation exchange column by isocratic elution. The method reduces the digestion time to less than 1 h and eliminates the distillation and titration steps of the Kjeldahl method, thereby reducing the analysis time significantly and improving precision and accuracy. To determine protein nitrogen in samples containing non-protein nitrogen, proteins are precipitated by a mixture of deoxycholate and trichloroacetic acid and the precipitates are analyzed after dissolving in KOH. The method is particularly useful for biological samples that are limited and can also be applied to food, environmental, and other materials., (Published by Elsevier Inc.) more...
- Published
- 2016
- Full Text
- View/download PDF
9. Evaluation of growth based rapid microbiological methods for sterility testing of vaccines and other biological products.
- Author
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Parveen S, Kaur S, David SA, Kenney JL, McCormick WM, and Gupta RK
- Subjects
- Adenosine Triphosphate metabolism, Bacteria growth & development, Bacteria metabolism, Carbon Dioxide metabolism, Fungi growth & development, Fungi metabolism, Sensitivity and Specificity, Biological Products standards, Chemistry Techniques, Analytical methods, Drug Contamination, Microbiological Techniques methods, Technology, Pharmaceutical methods, Vaccines standards
- Abstract
Most biological products, including vaccines, administered by the parenteral route are required to be tested for sterility at the final container and also at various stages during manufacture. The sterility testing method described in the Code of Federal Regulations (21 CFR 610.12) and the United States Pharmacopoeia (USP, Chapter <71>) is based on the observation of turbidity in liquid culture media due to growth of potential contaminants. We evaluated rapid microbiological methods (RMM) based on detection of growth 1) by adenosine triphosphate (ATP) bioluminescence technology (Rapid Milliflex(®) Detection System [RMDS]), and 2) by CO(2) monitoring technologies (BacT/Alert and the BACTEC systems), as alternate sterility methods. Microorganisms representing Gram negative, Gram positive, aerobic, anaerobic, spore forming, slow growing bacteria, yeast, and fungi were prepared in aliquots of Fluid A or a biological matrix (including inactivated influenza vaccines) to contain approximately 0.1, 1, 10 and 100 colony forming units (CFU) in an inoculum of 10 ml. These preparations were inoculated to the specific media required for the various methods: 1) fluid thioglycollate medium (FTM) and tryptic soy broth (TSB) of the compendial sterility method (both membrane filtration and direct inoculation); 2) tryptic soy agar (TSA), Sabouraud dextrose agar (SDA) and Schaedler blood agar (SBA) of the RMDS; 3) iAST and iNST media of the BacT/Alert system and 4) Standard 10 Aerobic/F and Standard Anaerobic/F media of the BACTEC system. RMDS was significantly more sensitive in detecting various microorganisms at 0.1CFU than the compendial methods (p<0.05), whereas the compendial membrane filtration method was significantly more sensitive than the BACTEC and BacT/Alert methods (p<0.05). RMDS detected all microorganisms significantly faster than the compendial method (p<0.05). BacT/Alert and BACTEC methods detected most microorganisms significantly faster than the compendial method (p<0.05), but took almost the same time to detect the slow growing microorganism P. acnes, compared to the compendial method. RMDS using SBA detected all test microorganisms in the presence of a matrix containing preservative 0.01% thimerosal, whereas the BacT/Alert and BACTEC systems did not consistently detect all the test microorganisms in the presence of 0.01% thimerosal. RMDS was compatible with inactivated influenza vaccines and aluminum phosphate or aluminum hydroxide adjuvants at up to 8 mg/ml without any interference in bioluminescence. RMDS was shown to be acceptable as an alternate sterility method taking 5 days as compared to the 14 days required of the compendial method. Isolation of microorganisms from the RMDS was accomplished by re-incubation of membranes with fresh SBA medium and microbial identification was confirmed using the MicroSEQ Identification System. BacT/Alert and BACTEC systems may be applicable as alternate methods to the compendial direct inoculation sterility method for products that do not contain preservatives or anti-microbial agents., (Published by Elsevier Ltd.) more...
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- 2011
- Full Text
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10. Evolving values in community-based long-term care services for Japanese Americans.
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Young HM, McCormick WM, and Vitaliano PP
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- Aged, Aged, 80 and over, Caregivers psychology, Family psychology, Female, Health Knowledge, Attitudes, Practice, Humans, Japan ethnology, Male, Motivation, Nursing Methodology Research, Surveys and Questionnaires, United States, Asian psychology, Attitude to Health ethnology, Community Health Services statistics & numerical data, Health Services for the Aged statistics & numerical data, Long-Term Care statistics & numerical data, Social Change, Social Values
- Abstract
This study used grounded theory to explore how long-term care services are perceived and what factors influence family caregiving and long-term care service utilization choices among Japanese Americans. Family and generational perspectives elucidated a dialectic between forces of integration into the broader culture, and reconnection with the culture of origin within the context of powerful ethnically based historical and generational experiences. This study describes the evolution of the values underlying service delivery and family expectations and demonstrates the dynamic relationships among cultural expectations, historical context, and service evolution for a group of members involved in the caregiving experience. more...
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- 2002
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11. Photoaffinity labeling of the hormone binding site of neurophysin.
- Author
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Abercrombie DM, McCormick WM, and Chaiken IM
- Subjects
- Amino Acids analysis, Animals, Binding Sites, Cattle, Neurophysins isolation & purification, Peptide Fragments analysis, Trypsin, Affinity Labels pharmacology, Azides, Neurophysins metabolism, Oligopeptides pharmacology, Pituitary Gland metabolism, Pituitary Gland, Anterior metabolism
- Abstract
The chemical structure of the hormone binding region of the neurophysins has been investigated by photoaffinity labeling with the photolabile tripeptide, L-[methyl-3H]Met-L-Tyr-p-azido-L-Phe amide. Photolysis of the photoaffinity tripeptide in the presence of bovine neurophysin I and II and a human neurophysin II led to approximately equal extents of covalent incorporation of radioactivity into protein. Photolabeled bovine neurophysin II was fractionated into binding site derivatized protein and nonbinding site derivatized protein by affinity chromatography, with results of amino acid and radiolabel analysis of the hormone binding site blocked protein indicating that 1 mol of tripeptide was covalently incorporated/mol of protein. Tyrosine 49 was the only protein amino acid modified in the binding site photolabeling reaction as assessed by peptide mapping of the performic acid oxidized and trypsin-digested photolabeled protein using reverse phase high performance liquid chromatography. Modification of the single neurophysin tyrosine also was found by amino acid analysis of performic acid oxidized photolabeled bovine neurophysin II. The covalent bond formed in neurophysin upon photolysis was cleaved by either exhaustive acid hydrolysis or reduction-carboxymethylation without loss of the protein amino acid residues and by performic acid oxidation with loss of both protein and tripeptide tyrosine residues. These overall data indicate that tyrosine 49 is the probable site for specific covalent attachment of the photoaffinity tripeptide. Assuming that the tripeptide binding site is the high affinity hormone binding site reported for the neurophysins, this conclusion argues that tyrosine 49 is close to or within this site. more...
- Published
- 1982
12. Characterization of the major forms of human calcitonin in tissue and serum.
- Author
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Dermody WC, Rosen MA, Ananthaswamy R, McCormick WM, and Levy AG
- Subjects
- Calcitonin blood, Chromatography, Affinity, Electrophoresis, Polyacrylamide Gel, Humans, Immunoelectrophoresis, Isoelectric Point, Lectins, Lymphatic Metastasis, Macromolecular Substances, Molecular Weight, Calcitonin metabolism, Carcinoma metabolism, Thyroid Gland metabolism, Thyroid Neoplasms metabolism
- Published
- 1981
- Full Text
- View/download PDF
13. Expression of multivalency in the affinity chromatography of antibodies. Appendix: Derivation and evaluation of equations for independent bivalent interacting systems in quantitative affinity chromatography.
- Author
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Eilat D, Chaiken IM, and McCormick WM
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- Antibody Affinity, Antigen-Antibody Reactions, Binding Sites, Chromatography, Affinity methods, Immunoglobulin Fab Fragments, Macromolecular Substances, Mathematics, Models, Biological, Phosphorylcholine, Plasmacytoma, Antibodies, Immunoglobulin A, Myeloma Proteins
- Abstract
The expression of multivalency in the interaction of antibody with immobilized antigen was evaluated by quantitative affinity chromatography. Zones of radioisotopically labeled bivalent immunoglobulin A monomer derived from the myeloma protein TEPC 15 were eluted from columns of phosphorylcholine-Sepharose both in the absence and presence of competing soluble phosphorylcholine. At sufficient immobilized phosphorylcholine concentration, the variation of elution volume of bivalent monomer with soluble ligand was found to deviate from that observed for the univalent binding of the corresponding Fab fragment. In addition, the apparent binding affinity of the bivalent monomer increased with immobilized antigen density. Use of equations relating the variation of elution volume with free ligand concentration for a bivalent binding protein allowed calculation of microscopic single-site binding parameters for the bivalent monomeric antibody to both immobilized and soluble phosphorylcholine. The chromatographic data not only demonstrate the effect of multivalency on apparent binding affinity but also offer a relatively simple means to measure microscopic dissociation constants for proteins participating in bivalent interactions with their ligands. more...
- Published
- 1979
- Full Text
- View/download PDF
14. Design of a photoaffinity label for the hormone binding site of neurophysin.
- Author
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Klausner YS, McCormick WM, and Chaiken IM
- Subjects
- Animals, Cattle, Peptides chemical synthesis, Phenylalanine analogs & derivatives, Photolysis, Neurophysins, Receptors, Cell Surface
- Abstract
The photolabile peptide, L-methionyl-L-tyrosyl-p-azido-L-phenylalaninamide, was synthesized by solution methods. This peptide, as well as the analogous species containing tritiated methionine, were found to bind reversibly and specifically, in the dark, to bovine neurophysin II. The dissociation constant, stoichiometry, and pH-dependence of this noncovalent interaction are typical of those properties for hormone (oxytocin) and hormone-like ligand binding to neurophysin II. Under photolytic conditions, methionyl-tyrosyl-p-azidophenylalaninamide causes irreversible inhibition of the noncovalent ligand binding activity of neurophysin II. This inactivation was achieved to the extent of about 90%. Both the dark and light (photolytic) interactions of the photolabile peptide with neurophysin II indicate its reaction at the hormone binding site of the protein and thus its potential use to identify amino acid residues at this site by covalent photoaffinity labelling. more...
- Published
- 1978
15. Bactericidal antibody in genital infection due to Neisseria gonorrhoeae.
- Author
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Kasper DL, Rice PA, and McCormick WM
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- Blood Bactericidal Activity, Convalescence, Epididymitis immunology, Female, Humans, Immunologic Techniques, Male, Antibodies, Bacterial biosynthesis, Gonorrhea immunology, Neisseria gonorrhoeae immunology
- Abstract
An assay of bactericidial antibody has been developed to study the host response to infection with Neisseria gonorrhoeae. This test for antibody was performed on the sera of women who were exposed to N. gonorrhoeae but who did not become infected, of patients with various types of genital infection with N. gonorrhoeae, and of a small number of individuals with no history of gonorrhea. Antibody was found in the sera of less than 31% of men and women with uncomplicated gonococcal infection. Prolonged mucosal infection with the gonococcus (greater than 33 days) correlated with the presence of bactericidal antibody. Bactericidal antibody was not detected in 95% of the specimens of acute-phase serum obtained from women with gonococcal pelvic inflammatory disease. The convalescent-phase sera of 70% of women with clinically severe pelvic inflammatory disease showed a rise in titer of bactericidal antibody to the infecting strain of N. gonorrhoeae, whereas only 11% of the convalescent-phase sera of women with mild or moderately severe disease showed a similar rise. more...
- Published
- 1977
- Full Text
- View/download PDF
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