Vitamins and Coenzymes, Part J
- 1st Edition, Volume 280 - June 16, 1997
- Editors: Donald B. McCormick, John N. Abelson, John W. Suttie, Melvin I. Simon, Conrad Wagner
- Language: English
- Hardback ISBN:9 7 8 - 0 - 1 2 - 1 8 2 1 8 1 - 4
- eBook ISBN:9 7 8 - 0 - 0 8 - 0 8 8 3 9 2 - 2
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… Read more
Purchase options
Institutional subscription on ScienceDirect
Request a sales quoteThe 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.
- 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
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.
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.
- No. of pages: 496
- Language: English
- Edition: 1
- Volume: 280
- Published: June 16, 1997
- Imprint: Academic Press
- Hardback ISBN: 9780121821814
- eBook ISBN: 9780080883922
DM
Donald B. McCormick
Affiliations and expertise
Emory University, Atlanta, Georgia, U.S.A.JA
John N. Abelson
Affiliations and expertise
California Institute of Technology, Division of Biology, Pasadena, U.S.A.JS
John W. Suttie
Affiliations and expertise
University of Wisconsin, Madison, U.S.A.MS
Melvin I. Simon
Affiliations and expertise
The Salk Institute, La Jolla, CA, USACW
Conrad Wagner
Affiliations and expertise
Department of Veterans Affairs Medical Center and Vanderbilt University, Nashville, Tennessee, U.S.A.Read Vitamins and Coenzymes, Part J on ScienceDirect