Vitamins and coenzymes

Author(s)

• McCormick, Donald B.
• Wright, Lemuel D
• Chytil, Frank
• Suttie, J. W. (John Weston)
• Wagner, Conrad

Bibliographic Information

Vitamins and coenzymes

edited by Donald B. McCormick and Lemuel D. Wright

（Methods in enzymology / editors in chief, Sidney P. Colowick, Nathan O. Kaplan, v. 18, 62, 66-67, 122-123, 279-282）

Academic Press, 1970-

• pt. A
• pt. B
• pt. C
• pt. D
• pt. E
• pt. F
• pt. G
• pt. H
• pt. I
• pt. J
• pt. K
• pt. L

Note

Pt. G-H edited by Frank Chytil, Donald B. McCormick

Pt. I-L edited by Donald B. McCormick, John W. Suttie, Conrad Wagner

Includes bibliographical references and indexes

Description and Table of Contents

Volume

pt. A ISBN 9780121818791

Description

The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences.

Volume

pt. B ISBN 9780121818807

Description

The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences.

Volume

pt. C ISBN 9780121818821

Description

The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences.

Volume

pt. D ISBN 9780121819620

Description

The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today truly an essential publication for researchers in all fields of life sciences.

Volume

pt. E ISBN 9780121819668

Description

The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences.

Volume

pt. F ISBN 9780121819675

Description

The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences.

Volume

pt. G ISBN 9780121820220

Description

The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences.

Volume

pt. H ISBN 9780121820237

Description

The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences.

Volume

pt. I ISBN 9780121821807

Description

This volume of Methods in Enzymology and its companion volumes 280, 281, and 282 present new methods and their modifications developed in the past decade plus the more recently acquired knowledge on the functional and metabolic aspects of vitamins and coenzymes. They represent the only in-depth treatment dealing with methods related to vitamins and coenzymes, and contain methods that have never been grouped together before.

Table of Contents

• Ascorbic Acid: E. Kimoto, S. Terada, and T. Yamaguchi, Analysis of Ascorbic Acid, Dehydroascorbic Acid, and Transformation Products by Ion-Pairing High Performance Liquid Chromatography with Multiwavelength Ultraviolet and Electrochemical Detection. J.C. Deutsch, Gas Chromatographic/Mass Spectrometric Measurements of Ascorbic Acid and Analysis of Ascorbic Acid Degradation in Solution. K. Yagi and M. Nishiskimi, Expression of Recombinant L-Gulono-gamma-lactone Oxidase. E. Maellaro, B. Del Bello, L. Sugherini, M. Comporti, and A.F. Casini, Purification and Characterization of Gluathione-Dependent Dehydroascorbic Reductase from Rat Liver. A.S. Kolhekar, R.E. Mains, and B.A. Eipper, Peptidylglycine alpha-Amidating Monooxygenase: An Ascorbate-Requiring Enzyme. M. Levine, S. Rumsey, and Y. Wang, Principles Involved in Formulating Recommendations for Vitamin C Intake: A Paradigm for Water-Soluble Vitamins. Thiamin: Phosphates and Analogs: V. Fayol, High-Performance Liquid Chromatography Determination of Total Thiamin in Biological and Food Products. C.M.E. Tallaksen, T. Bohmer, J. Karlsen, and H. Bell, Determination of Thiamin and Its Phosphate Esters in Human Blood, Plasma, and Urine. J. Gerrits, H. Eidhof, J.W.I. Brunnekreeft, and J. Hessels, Determination of Thiamin and Thiamin Phosphates in Whole Blood by Reversed-Phase Liquid Chromatography with Precolumn Derivtization. H.J. Mascher and C. Kikuta, High Performance Liquid Chromatography Determination of Total Thiamin in Human Plasma. D.T. Wyatt and R.E. Hillman, Cyanogen Bromide-Based Assay of Thiamin. K. Tazuya, K. Yamada, and H. Kumaoka, Isotopically Labled Precursors and Mass Spectrometry in Elucidating Biosynthesis of Pryimidine Moiety of Thiamin in Saccharomyces Cerevisiae. A. Iwashima, K. Nosaka, H. Nishimura, and F. Enjo, Thiamin Transporters in Yeast. G. Rindi, and U. Laforenza, In Vitro Systems for Studying Thiamin Transport in Mammals. A. Schellenberger, G. Habner, and H. Neef, Cofactor Designing in Functional Analysis of Thiamine Diphosphate Enzymes. Y. Suzuki and K. Uchida, Enzymatic Preparation of Derivatives of Thiamin
• O-beta-Galactosylthiamin and O-alpha-Glucosylthiamin. J. Teichert and R. Preiss, High-Performance Liquid Chromatography Methods for Determination of Lipoic and Dihydrolipoic Acid in Human Plasma. H. Kataoka, N. Hirabayashi, and M. Makita, Analysis of Lipoic Acid by Gas Chromotographywith Flame Photometric Detection. S.W. Jordan and J.E. Cronan, Jr., Biosynthesis of Lipoic Acid and Posttranslational Modification with Lipoic Acid in Escherichia coli. K. Fujiware, K. Okamura-Ikeda, and Y. Motokawa, Lipoate Addition to Acyltransferases of alpha-Keto Acid Dehydrogenase Complexes and H-Protein of Glycine Cleavage System. J. Quinn, Lipoylation of Acyltransferases Components of 2-Oxo Acid Dehydgogenase Complexes. J. Oizumi and K. Hayakawa, Purification and Properties of Brain Lipoamidase. K. Banno, Measurement of Pantothenic Acid and Hopantenic Acid by GC-Mass Spectroscopy. R. Padmakumar, R. Padmakumar, and R. Banerjee, Large-Scale Synthesis of Coenzymes A Esters. A. Abend and J. Retey, Synthesis of Nonhydrolyzable Acyl-Coenzyme A Analogs. K. Bartlett and M. Pourfarzam, Synthesis, Purifiction, and Characterization of Dicarboxylylmono-coenzyme A Esters. R.H. Lambalot and C.T. Walsh, Holo/Acyl-Carrier-Protein Synthase of Escherichia coli. Biotin and Derivatives: D.M. Mock, Determination of Biotin in Biological Fluids. N.G. Hentz and L.G. Bachas, Fluorophore-linked Assays for High-Performance Liquid Chromatography Postcolumn Reaction Detection of Biotin and Biocytin. G. Rehner and J. Stein, High-Performance Liquid Chromatographic Determination of Biotin in Biological Materials after Crown Ether-Catalyzed Fluorescence Derivitization with Pancyl Bromide. S. Lizano, S. Ramanathan, A. Feltus, A. Witkowski, and S. Daunert, Bioluminescence Competitive Binding Assays for Biotin Based on Photoprotein Aequorin. E.Z. Huang and Y. Rogers, Competitive Enzymatic Assay of Biotin. E.Z. Huang, L.J. Jones, S.M. Swan, and R.P. Haugland, Competitive Agglutination Assay of Biotin. D. Shiuan, C.-H. Wu, Y.-S. Chang, and R.-J. Chang, Competitive Enzyme-Linked Immunosorbent Assay for Biotin. P. Baldet, C. Alban, and R. Douce, Biotin Synthesis in Higher Plants. K. Hatakeyama, M. Kobayashi, and H. Yukawa, Analysis of Biotin Biosynthesis Pathway in Coryneform Bacteria Brevibacterium flavum. D.H. Flint and R.M. Allen, Purification and Characterization of Biotin Synthases. B.T.S. Bui and A. Marquet, Biotin Synthase of Bacillus Sphaericus.D. Beckett and B.W. Matthews, Escherichia coli Repressor of Biotin Biosynthesis. G. Schneider and Y. Linqvist, Structure of ATP-Dependent Carboxylase, Dethiobiotin Synthase. Y. Suzuki and K. Narisawa, Purification and Properties of Bovine and Human Holocarboxylase Synthetases. D.L. Dyer and H.M. Said, Biotin Uptake in Cultured Cell Lines. Y. Xu and D. Beckett, Biotinyl-5-Adenylate Synthesis Catalyzed by Escherichia coli Repressor of Biotin Biosynthesis. J. Hymes, K. Fleischlauer, and B. Wolf, Biotinidase in Serum and Tissues. K. Hayakawa, K. Yoshikawa, J. Oizumi, and K. Yamauchi, Determination of Biotinidase Activity with Biotinyl-6-aminoquinoline as Substrate. E. Livaniou, S.E. Kakabakos, G.P. Evangelatos, S.A. Evangelatos, and D.S. Ithakissios, Determination of Serum Biotinidase Activity with Radioiodinated Biotinylamide Analogs. F. Kohen, H. Bagci, G. Barnard, E. Bayer, B. Gayer, D. Schindler, E. Ainbinder, and M. Wilchek, Preparation and Properties of Anti-Biotin Antibodies. H.B. White III, Competitive Binding Assays for Biotin-Binding Proteins. Subject Index. Author Index.

Volume

pt. J ISBN 9780121821814

Description

The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. More than 270 volumes have been published (all of them still in print) and much of the material is relevant even today--truly an essential publication for researchers in all fields of life sciences.

Table of Contents

Pyridoxine, Pyridoxamine, Pyridoxal: Analogs and Derivatives: H. Tsuge, Determination of Vitamin B 6 Vitamers and Metabolites in Biological Sample. H.J. Mascher, High-Performance Liquid Chromatography Determination of Total Pyridoxal in Human Plasma. J.D. Mahuren and S.P. Coburn, Determination of 5-Pyridoxic Acid, 5-Pyridoxic Acid Lactone, and other Vitamin B6 Compounds by Cation-Exchange High-Performance Liquid Chromatography. D.E. Metzler, Nuclear Magnetic Resonance in Study of Active Sites of Pyridoxal-Dependent Enzymes. T. Fukui and K. Tanizawa, Synthesis and Application of Pyridoxal Polyphosphoryl Derivatives as Active-Site Probes for Nucleotide-Binding Enzymes. S. Stein and T. Zhu, Preparation of Vitamin B6-Peptide and Vitamin B6-Peptide-Oligonucleotide Conjugates. J.F. Gregory III and H. Nakano, Preparation of Nonlabeled, Tritiated, and Deuterated Pyridoxine 5-beta-D-Glucoside and Assay of Pyridoxine-5-beta-D-Glucoside Hydrolase. Y. Suzuki, Y. Doi, K. Uchida, and H. Tsuge, Enzymatic Preparation of Pyridoxine 4- and 5-alpha-D-Glucosides. Y. Suzuki and K. Uchida, Formation of Beta-Galactosides of Pyridoxine using Sporobolomyces singularis. Carbonyl Coenzymes: Pyruvyl Enzymes and Quinoproteins: W. Dowhan, Phosphatidylserine Decarboxylases: Pyruvoyl-Dependent Enzymes from Bacteria to Mammals. M. Misset-Smits, A.J.J. Olshoorn, A. Dewanti, and J.A. Duine, Production, Assay, and Occurrence of Pyrroloquinoline Quinone. C. Hartmann and W.S. McIntire, Amine-Oxidizing Quinoproteins. O. Suzuki and T. Kumazawa, Gas Chromatographic/Mass Spectrometric Analysis of Pyrroloquinoline Quinone. H. Narita and E. Morishita, Monoclonal Antibodies Specific to Pyrroloquinoline Quinone. Nicotinic Acid: Analogs and Coenzymes: A. Klemm, T. Steiner, U. Flitgen, G.A. Cumme, and A. Horn, Determination, Purification, and Characterization of alpha-NADH and alpha-NADPH. R.F. Colman, Affinity Labels for NaD(P)-Specific Sites. C.M. Ensor and H.-H. Tai, Photoaffinity Labeling of NAD+-Linked Enzymes. V. Micheli and S. Sestini, Determining NAD Synthesis in Erythrocytes. E.L. Jacobson and M.K. Jacobson, Tissue NAD as Biochemical Measure of Niacin Status in Humans. R.M. Graeff, T.F. Walseth, and H.C. Lee, Radioimmunoassay for Measuring Endogenous Levels of Cyclic ADP-Ribose in Tissues. G. Magni, M. Emanuelli, A. Amici, N. Raffaelli, and S. Ruggieri, Purification of Human Nicotinamide-Mononucleotide Adenylyltransferase. G. Magni, M. Emanuelli, A. Amici, N. Raffaelli, and S. Ruggieri, Nicotinamide-Mononucleotide Adenylyltransferases from Yeast and Other Microorganisms. J. Zhang, Use of Biotinylated NAD to Label and Purify ADP-Ribosylated Proteins. M.K. Jacobson, D.L. Coyle, C.Q. Vu, H. Kim, and E.L. Jacobson, Preparation of Cyclic ADP-Ribose, 2'-Phospho-Cyclic ADP-Ribose, and Nicotinate Adenine Dinucleotide Phosphate: Possible Second Messengers of Calcium Signaling. D. Cervantes-Laurean, E.L. Jacobson, and M.K. Jacobson, Preparation of Low Molecular Weight Model Conjugates for ADP-Ribose Linkages to Protein. T.F. Walseth, L. Wong, R.M. Graeff, and H.C. Lee, Bioassay for Determining Endogenous Levels of ADP-Ribose. T.F. Walseth, R. Aarhus, M.E. Gurnack, L. Wong, H.A. Breitinger, K.R. Gee, and H.C. Lee, Preparation of Cyclic ADP-Ribose Antagonists and Caged Cyclic ADP-Ribose. H. Okamoto, S. Takasawa, A. Tohgo, K. Nata, I. Kato, and N. Noguchi, Synthesis and Hydrolysis of Cyclic ADP-Ribose by Human Leukocyte Antigen CD38: Inhibition of Hydrolysis by ATP and Physiological Significance. C.B. Munshi, K.B. Fryxell, H.C. Lee, and W.D. Branton, Large-Scale Production of Human CD38 in Yeast by Fermentation. H.C. Lee, R.M. Graeff, C.B. Munshi, T.F. Walseth, and R. Aarhus, Large-Scale Purification of Aplysia ADP-Ribosylcyclase and Measurement of Its Activity by a Fluorimetric Assay. Flavins and Derivatives: S.-I. Huang, M.J. Caldwell, and K.L. Simpson, Urinary Riboflavin Determination by C18 Reversed-Phase, Open-Column Chromatography. K. Matsui and S. Kasai, Chemical Synthesis and Properties of 7alpha-Hydroxyriboflavin. A.F. Backmann, V. Wray, and A. Stocker, Synthesis of N6-(2-Aminoethyl)-FAD, N6-(6-Carboxyhexyl)-FAD, and Related Compounds. G. Richter, C. Krieger, R. Volk, K. Kis, H. Ritz, E. Gitze, and A. Bacher, Biosynthesis of Riboflavin: 3,4-Dihydroxy-2-butanone-4-phosphate Synthase. A. Bacher, G. Richter, H. Ritz, S. Eberhardt, M. Fischer, and C. Krieger, Biosynthesis: Riboflavin GTP Cyclohydrolase II, Deaminase, and Reductase. A. Bacher, S. Eberhardt, M. Fischer, S. Mirtl, K. Kis, K. Kugelbrey, J. Scheuring, and K. Schott, Biosynthesis of Riboflavin: Lumazine Synthase and Riboflavin Synthase. G. Rindi and G. Gastaldi, Measurements and Characteristics of Intestinal Riboflavin Transport. D.B. McCormick, M. Oka, D.M. Bowers-Komro, Y. Yamada, and H.A. Hartman, Purification and Properties of FAD Synthetase from Liver. K. Decker and R. Brandsch, Determining Covalent Flavinylation. R.S-F. Lee and H.C. Ford, Purification and Characterization of 5-Nucleotidase/FAD Pyrophosphatase from Human Placenta. Y.V.S.N. Murthy and V. Massey, Syntheses and Application of Flavin Analogs as Active-Site Probes for Flavoproteins. Subject Index. Author Index.

Volume

pt. K ISBN 9780121821821

Description

General Description of the Volume:This volume of Methods in Enzymology and its companion Volumes 279, 280, and 282 present new methods and their modifications developed in the past decade plus the more recently acquired knowledge on the functional and metabolic aspects of vitamins and coenzymes. They represent the only in-depth treatment dealing with methods related to vitamins and coenzymes, and contain methods that have never been grouped together before.General Description of the Series:The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.

Table of Contents

Folic Acid:S.W. Bailey and J.E. Ayling, Total Chemical Synthesis of Chirally Pure (6S)-Tetrahydrofolic Acid.P.J. Bagley and J.Selhub, Analysis of Folates Using Combined Affinity and Ion Pair Chromatography.C.R. Santhosh-Kumar and J.F. Kolhouse, Molar Quantitation of Folates by Gas Chromatograph-Mass Spectrometry.D.W. Horne, Microbiological Assay of Folates in 96-Well Microtiter Plates.A.M. Molloy and J.M. Scott, Microbiological Assay for Serum, Plasma, and Red Cell Folate Using Cryopreserved Microtiter Plate Method.E.R. Werner, H. Wachter, and G. Werner-Felmayer, Determination of Tetrahydrobiopterin Biosynthetic Activities by High-Performance Liquid Chromatography with Fluorescence Detection.R.J. Leeming, Microtiter Plate Assay for Biopterin Using Cryopreserved Crithidia fasciculata. J. McPartlin and J.M. Scott, Identification and Assay of Folate Catabolites in Human Urine.V. Schirch, Enzymatic Determination of Folylpolyglutamate Pools.V. Schirch, Synthesis and Interconversion of Reduced Folylpolyglumates.A.L. Fitzhugh and R.K. Akee, Chemical Synthesis of (6S)-5-Formyl-5,6,7,8-tetrahydropteroyl-poly-gamma-L-glutamates.J. Fan and F.M. Huennekens, Biotin Derivatives of Folate Compounds: Synthesis and Utilization for Visualization and Affinity Purification of Folate Transport Proteins.C.M. Pfeiffer and J.F. Gregory, III, Preparation of Stable Isotopically Labeled Folates for in Vivo Investigation of Folate Absorption and Metabolism.S. Milstien, Interconversion of 6- and 7-Substituted Tetrahydropterins via Enzyme-Generated 4a-Hydroxytetrahydroprotein Intermediates.M. Hoshiga and K. Hatakeyama, Enzymatic Synthesis of 6R-U-14C Tetrahydrobiopterin from U-14CGTP.R.J. Cook, Use of 10-Formyldideazafolate as Substrate for Rat 10-Formyltetrahydrofolate.I. Atkinson, T. Garrow, A. Brenner, and B. Shane, Human Cytosolic Folylpoly-gamma-Glutamate Synthase.H.C. Imeson and E.A. Cossins, Folylpolyglutamate Synthase from Higher Plants.V. Schirch, Purification of Folate-Dependent Enzymes from Rabbit Liver.J. Jolivet, Human 5,10 Methenyltetrahydrofolate Synthetase.R.E. MacKenzie, Mitochondrial NAD-Dependent Methylenetetrahydrofolate Dehydrogenase-Methenyltetrahydrofolate Cyclohydrolase.D.R. Appling and M.G. West, Monofunctional NAD-Dependent 5,10-Methylenetetrahydrofolate Dehydrogenase from Saccharomyces cerevisiaeR. Banerjee, Z. Chen, and S. Gulati, Methionine Synthase from Pig Liver.J.T. Jarrett, K. Fluhr, C. Goulding, S. Huang, and R.G. Matthews, Purification and Assay of Cobalamin-Dependent Methionine Synthase from Escherichia coli. H. Zalkin, Formyltetrahydrofolate Hydrolase from Escherichi coli.D.R. Appling, E. Kastanos, L.B. Pasternack, and Y.Y. Woldman, Use of 13C Nuclear Magnetic Resonance to Evaluate Metabolic Flux through Folate One-Carbon Pools in Saccharomyces cerevisiae.Vitamin B12 and Cobalamins:C.B. Grisson and E. Natarajan, Use of Magnetic Field Effects to Study Coenzyme B12 Dependent Reactions.D.P. Sundin and R.H. Allen, Analysis of Cobalamin and Cobalamin Analogs by Gas Chromatography-Mass Spectrometry.M.M. Gordon, G. Russell-Jones, and D.H. Alpers, Expression of Functional Intrinsic Factor Using Recombinant Baculovirus.S.P. Rothenberg and E.V. Quadros, Quantitative Methods for Measurement of Transcobalamin II.L. Qian, E.V. Quadros and S.P. Rothenberg, Molecular Methods for Analysis and Expression of Transcobalamin II.S. Bose and B. Seetharam, Purification, Membrane Expression, and Interactions of Transcobalamin II Receptor.F. Watanabe and Y. Nakano, Purification and Characterization of Aquacobalamin Reductase from Euglena gracilis. F. Watanabe and Y. Nakano, Purification and Characterization of Aquacobalamin Reductases from Mammals.Heme:P.M. Shoolingin-Jordan, J.E. LeLean, and A.J. Lloyd, Continous Coupled Assay for 5-Aminolevulinate Synthase.P.M. Shoolingin-Jordan, M.J. Warren, and S.J. Awan, Dipyrromethane Cofactor Assembly of Porphobilinogen Deaminase: Formation of Apoenzyme and Preparation of Holoenzyme.P.M. Shoolingin-Jordan and R. Leadbeater, Coupled Assay for Uroporphyrinogen III Synthase.H.A. Dailey and T.A. Dailey, Expression and Purification of Mammalian 5-Aminolevulinate Synthase.H.A. Dailey and T.A. Dailey, Expression, Purification, and Characterization of Mammalian Protoporphyrinogen Oxidase.A.G. Roberts and G.H. Elder, Purification and Properties of Uroporphyrinogen Decarboxylase from Human Erythrocytes.T. Yoshinaga, Purification and Properties of Coproporphyrinogen III Oxidase from Bovine Liver.P. Labbe, Purification and Properties of Coproporphyrinogen III Oxidase from Yeast.V.M. Sellers and H.A. Daily, Expression, Purification and Characterization of Recombinant Mammalian Ferrochelatase.Miscellaneous Vitamins and Coenzymes:R.H. White, Structural Characterization of Modified Folates in Archaea.Methodologies Broadly Applicable to Vitamins and Coenzymes:J. Zempleni, Biokinetic Analysis of Vitamin Absorption and Disposition in Humans.M. Levine, S.C. Rumsey, Y. Wang, J. Park, O. Kwon, and N. Amano, In Situ Kinetics: An Approach to Recommended Intake of Vitamin C.Subject Index.Author Index.

Volume

pt. L ISBN 9780121821838

Description

The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. More than 270 volumes have been published (all of them still in print) and much of the material is relevant even today--truly an essential publication for researchers in all fields of life sciences.

Table of Contents

Vitamin A: A.W. Norris and E. Li, Generation and Characterization of Cellular Retinoic Acid-Binding Proteins from Escherichia coli Expression System. M. Clagett-Dame and J.J. Repa, Generating and Characterizing Retinoid Receptors from Escherichia coli and Insect Cell Expression Systems. E.A. Allegretto and R.A. Heyman, Expression and Characterization of Retinoid Receptors in Yeast. A. Rowe and P.M. Brickell, Use of in Situ Hybridization Techniques to Study Embryonic Expression of Retinoid Receptors and Binding Proteins. N. Ferrari, G. Vidali, and U. Pfeffer, Use of Quantitative PCR to Study Retinoid Receptor Expression. L. Zhou, G. Otulakowski, and C.Y. Lau, Use of Quantitative PCR to Study Cellular Retinoic Acid Binding Protein-II mRNA Expression in Human Skin. L. Wojnowski and A. Zimmer, Use of Transgenic Mice to Study Activation of Retinoic Acid-Responsive Promoters. M. Saitou, T. Tanaka, and A. Kakizuka, Use of Transgenic Mice to Eliminate Retinoic Acid Receptor Function in Specific Tissues. M. Wagner, Use of Reporter Cells to Study Endogenous Retinoid Sources in Embryonic Tissues. P.K. Tadikonda and H.F. DeLuca, Preparation of Radiolabeled9-cis- and all-trans-Retinoids. X-D. Wang and N.I. Krinsky, Identification and Quantification of Retinoic Acid and Other Metabolites from (-Carotene Excentric Cleavage in Human Intestine in Vitro and Ferret Intestine in Vivo. R.S. Parker, J.T. Brenna, J.E. Swanson, K.J. Goodman, and B. Marmor, Assessing Metabolism of (-[13C] Carotene Using High Precision Isotope Ratio Mass Spectrometry. G. Tang, B.A. Andrien, G.G. Donikowski, and R.M. Russell, Atmospheric Pressure Chemical Ionization and Electron Capture Negative Chemical Ionization Mass Spectrometry in Studying (-Carotene Conversion to Retinol in Humans. Vitamin D: R. Ray and M.F. Holick, Synthesis of [3(-3H]Vitamin D3 and 1(,25-Dihydroxy[1(-3H]Vitamin D3. M.J. Beckman and H.F. DeLuca, Assay of 1,25-Dihydroxyvitamin D3 from Serum Samples: Use of Receptor Binding or Enzyme Coupled Reporter Analysis. B.W. Hollis, Quantitation of 25-Hydroxyvitamin D and 1,25-Dihydroxyvitamin D by Radioimmunoassay Using Radioiodinated Tracers. Y. Ohyama, S-I. Hayashi, E. Usui, M. Noshiro, and K-I. Okuda, Assay of Vitamin D Derivatives and Purification of Vitamin D Hydroxylases. M.J. Beckman and H.F. DeLuca, Assay of25-Hydroxyvitamin D 1(-Hydroxylase and 24-Hydroxylase. M. Noshiro, Y. Ohyama, E. Usui, M. Akiyoshi-Shibata, Y. Yabusaki, and K-I. Okuda, Molecular Cloning of Vitamin D3 Hydroxylases. T. Suda, E. Jimi, I. Nakamura, and N. Takahashi, Role of 1(,25-Dihydroxyvitamin D3 in Osteoclast Differentiation and Function. J.G. Meszaros and M.C. Farach-Carson, Assay of Direct Effect of 1,25-Dihydroxyvitamin D3 on Calcium Ion Influx into Cultured Osteoblasts. Vitamin E: A. Beharka, S. Redican, L. Leka, and S.N. Meydani, Vitamin E Status and Immune Function. M. Steiner, Inhibition of Platelet Adhesion as Functional Test for Vitamin E Status. N. Noguchi and E. Niki, Inhibition of Plasma Cholesterol Ester Hydroperoxide and Phosphatidylcholine Hydroperoxide Formation as Measures of Antioxidant Status. A.K. Dutta-Roy, (-Tocopherol-Binding Proteins: Purification and Characterization. M. Schultz, M. Leist, A. Elsner, and R. Brigelius-Flohe, (-Carboxyethyl-6-hydroxychroman as Urinary Metabolite of Vitamin E. Vitamin K: K.L. Berkner and B.A. McNally, Purification of Vitamin K-Dependent Carboxylase from Cultured Cells. B.C. Furie, A. Kuliopulos, D.A. Roth, I. Sugiura, C.T. Walsh, and B. Furie, Purification of Native Bovine Carboxylase and Expression and Purification of Recombinant Bovine Carboxylase. S-M. Wu, V.P. Mutucumarana, and D.W. Stafford, Purification of (-Glutamyl Carboxylase from Bovine Liver. R.J.T.J. Houben, B.A.M. Soute,and C. Vermeer, Assay of Vitamin K-Dependent Carboxylase Activity in Hepatic and Extrahepatic Tissues. F.J. Castellino and J-P. Geng, Expression of Human Anticoagulation Protein C and (-Carboxyglutamic Acid Mutants in Mammalian Cell Cultures. M.E. Benton and J.W. Suttie, Determination of Site-Specific (-Carboxyglutamic Formation by Vitamin K-Dependent Carboxylase Utilizing De-(-Carboxy Bone Gla Protein as Substrate. R. Wallin and T.M. Guenthner, Purification of Warfarin-Sensitive Vitamin K Epoxide Reductase. K.W. Davidson and J.A. Sadowski, Determination of Vitamin K Compounds in Plasma or Serum by High-Performance Liquid Chromatography Using Postcolumn Chemical Reduction and Fluorimetric Detection. P.T. McCarthy, D.L. Harrington, and M.J. Shearer, Assay of Phylloquinone in Plasma by High-Performance Liquid Chromatography with Electrochemical Detection. S.J. Hodges, Assay of Menaquinones in Plasma Utilizing Dual-Electrode Electrochemical Detection. Y. Usui, Assay of Phylloquinone and Menaquinones in Human Liver. S.L. Booth and J.A. Sadowski, Determination of Phylloquinone in Foods by High-Performance Liquid Chromatography. J.M. Conly, Assay of Menaquinones in Bacterial Cultures, Stool Samples, and Intestinal Cultures. Author Index. Subject Index.

by "Nielsen BookData"

Details

• NCID: BA00197940
• ISBN:
  • 0121818799
  • 0121818802
  • 0121818829
  • 0121819620
  • 0121819663
  • 0121819671
  • 012182022X
  • 0121820238
  • 0121821803
  • 0121821811
  • 012182182X
  • 0121821838
• LCCN: 72026903
• Country Code: us
• Title Language Code: eng
• Text Language Code: eng
• Place of Publication: New York ; Tokyo
• Pages/Volumes: v.
• Size: 24 cm
• Classification:
  • LCC : QP601
  • LCC : QP771
  • DC : 574.1/926
  • DC18 : 574.194
  • NLM : W1
  • NDLC : RA84
• Subject Headings:
  • LCSH : Vitamins
  • LCSH : Coenzymes
  • MESH : Coenzymes
  • MESH : Vitamins
• Parent Bibliography ID:
  • BA00197543