Vitamins and Coenzymes, Part I
- 1st Edition, Volume 279 - June 16, 1997
- Imprint: Academic Press
- Editors: John N. Abelson, Donald B. McCormick, Melvin I. Simon, John W. Suttie, Conrad Wagner
- Language: English
- Hardback ISBN:9 7 8 - 0 - 1 2 - 1 8 2 1 8 0 - 7
- eBook ISBN:9 7 8 - 0 - 0 8 - 0 8 8 3 9 1 - 5
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 recent… Read more
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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.
- This volume and its companion Volumes 280, 281, and 282 provide
- A collation of the most recent and useful methods for the identification, preparation, and quantification of vitamins and coenzymes
- Details on physical, chemical, and biological properties of vitamins and coenzymes
- Chemical and biological syntheses of vitamins, coenzymes, and their analogs
- Aspects of transport and metabolism of vitamins and coenzymes
Biochemists, Nutritionists, Cell Biologists, Pharmacologists, Molecular Biologists, and Physiologists
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.
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.
- Edition: 1
- Volume: 279
- Published: June 16, 1997
- Imprint: Academic Press
- Language: English
JA
John N. Abelson
Affiliations and expertise
California Institute of Technology, Division of Biology, Pasadena, U.S.A.DM
Donald B. McCormick
Affiliations and expertise
Emory University, Atlanta, Georgia, U.S.A.MS
Melvin I. Simon
Affiliations and expertise
The Salk Institute, La Jolla, CA, USAJS
John W. Suttie
Affiliations and expertise
University of Wisconsin, Madison, U.S.A.CW
Conrad Wagner
Affiliations and expertise
Department of Veterans Affairs Medical Center and Vanderbilt University, Nashville, Tennessee, U.S.A.Read Vitamins and Coenzymes, Part I on ScienceDirect