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 cerevisiae
R. 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.
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.
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.
@introbul:Key Features @bul:* This volume and its companion Volumes 279, 280, 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.
- No. of pages:
- © Academic Press 1997
- 25th July 1997
- Academic Press
- eBook ISBN:
- Hardcover ISBN:
@from:Praise for the Series @qu:"The Methods in Enzymology series represents the gold-standard." @source:--NEUROSCIENCE @qu:"Incomparably useful." @source:--ANALYTICAL BIOCHEMISTRY @qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." @source:--BIO/TECHNOLOGY @qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." @source:--CHEMISTRY IN INDUSTRY @qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." @source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS @qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." @source:--ENZYMOLOGIA @qu:"A series that has established itself as a definitive reference for biochemists." @source:--JOURNAL OF CHROMATOGRAPHY
Emory University, Atlanta, Georgia, U.S.A.
University of Wisconsin, Madison, U.S.A.
Department of Veterans Affairs Medical Center and Vanderbilt University, Nashville, Tennessee, U.S.A.
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA