Branched-chain amino acids

著者

• Harris, Robert A. (Robert Allison)
• Sokatch, J. R. (John Robert)

書誌事項

Branched-chain amino acids

edited by Robert A. Harris, John R. Sokatch

（Methods in enzymology / editors in chief, Sidney P. Colowick, Nathan O. Kaplan, v. 166, 324）

Academic Press, c1988-c2000

• [pt. A]
• pt. B

注記

Includes bibliographies and indexes

内容説明・目次

巻冊次

[pt. A] ISBN 9780121820671

内容説明

This volume includes chapters on the newest techniques for measuring metabolites of branched-chain amino acids, many new enzyme assays such as the measurement of isozymes of acetohydroxacid synthase, and the purification of recently described enzymes such as isovaleryl-CoA dehydrogenase.

目次

Analytical and Synthetic Methods: G. Livesey and P. Lund, Determination of Branched-Chain Amino and Keto Acids with Leucine Dehydrogenase. S.J. Yeaman, K.G. Cook, A.P. Bradford, and S.M.A. Jones, Analysis of Phosphorylation Sites on Branched-Chain 2-Ketoacid Dehydrogenase Complex. D.J. Aberhart and J.-A. Cotting, High-Performance Liquid Chromatographic Separation of (3R) and (3S)-/-Leucine Using Marfey's Reagent. D.J. Aberhart, High-Performance Liquid Chromatographic Separation of ~ga- and /-Leucine. A.L. Gasking, W.T.E. Edwards, A.H. Frohock, M. Elia, and G. Livesey, Quantitative High-Performance Liquid Chromatographic Analysis of Branched-Chain 2-Keto Acids in Biological Samples. O.A. Mamer and J.A. Montgomery, Determination of Branched-Chain 2-Hydroxy and 2-Keto Acids by Mass Spectrometry. P.L. Crowell, R.H. Miller and A.E. Harper, Measurement of Plasma and Tissue Levels of Branched-Chain ~ga-Keto Acids by Gas-Liquid Chromatography. J.A. Montgomery and O.A. Mamer, Determination of Methylmalonic Acid in Biological Fluids by Mass Spectrometry. B.E. Corkey, Analysis of Acyl Coenzyme A Esters in Biological Samples. M.T. King, P.D. Reiss, and N.W. Cornell, Determination of Short-Chain Coenzyme A Compounds by Reversed-Phase High-Performance Liquid Chromatography. K. Bartlett and A.G. Causey, Radiochemical High-Performance Liquid Chromatography Methods for the Study of Branched-Chain Amino Acid Metabolism. J.V. Schloss, R. Magolda, and M. Emptage, Synthesis of ~ga-lsopropylmalate, /-Isopropylmalate, and Dimethylcitraconate. R.A. LaRossa and T.K. Van Dyk, Utilization of Sulfometuron Methyl, an Acetolactate Synthase Inhibitor, in Molecular Biological and Metabolic Studies of Plants and Microbes. D.J. Danner, L.J. Elsas, and S. Litwer, Antibodies against Branched-Chain ~ga-Ketoacid Dehydrogenase Proteins for Use in Defining Human Mutations and Gene Isolation. R.A. Harris, M.J. Kuntz, and R. Simpson, Inhibition of Branched-Chain ~ga-Ketoacid Dehydrogenase Kinase by ~ga-Chloroisocaproate. Enzyme Assay. J.M. Poston, Measurement of Relative Carbon Flux in ~ga- and /-Keto Pathways of Leucine Metabolism. J.M. Poston, Assay of Leucine 2, 3-Aminomutase. D.T. Chuang and R.P. Cox, Enzyme Assays with Mutant Cell Lines of Maple Syrup Urine Disease. D.T. Chuang, Assays of E1 and E2 Components of Branched-Chain Ketoacid Dehydrogenase Complex. Y. Ikeda and K. Tanaka, Mutant Isovaleryl-CoA Dehydrogenase in Isovaleric Acidemia Cells: Assay of Activity and Molecular Characterization. J. Espinal, M. Beggs, and P.J. Randle, Assay of Branched-Chain ~ga-Ketoacid Dehydrogenase Kinase in Mitochondrial Extracts and Purified Branched-Chain ~ga-Ketoacid Dehydrogenase Complexes. P.A. Patston, J. Espinal, M. Beggs, and P.J. Randle, Assay of Total Complex and Activity State of Branched-Chain ~ga-Ketoacid Dehydrogenase Complex and of Activator Protein in Mitochondria, Cells, and Tissues. G.W. Goodwin, B. Zhang, R. Paxton, and R.A. Harris, Determination of Activity and Activity State of Branched-Chain ~ga-Ketoacid Dehydrogenase in Rat Tissues. K.P. Block, R.P. Aftring, M.G. Buse, and A.E. Harper, Estimation of Branched-Chain ~ga-Keto Acid Dehydrogenase Activation in Mammalian Tissues. K.M. Gibson, Assay of 3-Methylglutaconyl-CoA Hydratase. K.M. Gibson, Assay of 3-Hydroxy-3-Methylglutaryl-CoA Lyase. L.L. Searles and J.M. Calvo, Permeabilized Cell and Radiochemical Assays for /-Isopropylmalate Dehydrogenase. J.H. Jackson, Rapid Assay of Acetolactate Synthase in Permeabilized Bacteria. N. Gollop, Z. Barak, and D.M. Chipman, Assay of Products of Acetolactate Synthase. M. De Felice, G. Griffo, C.T. Lago, D. Limauro, and E. Ricca, Detection of the Acetolactate Synthase Isozymes I and III of Escherichia coli K12. T.K. Antonucci and D.L. Oxender, Transport of Branched-Chain Amino Acids in Escherichia coli. M.S. Kilberg, Transport of Branched-Chain Amino Acids and Their Corresponding 2-Keto Acids by Mammalian Cells. A. Hampel and R. Tritz, Leucine-tRNA Ligase Complexes. Enzymes. T.K. Korpela, Purification of Branched-Chain-Amino-Acid Aminotransferase from Pig Heart. R. Kido, Pancreatic Branched-Chain-Amino-Acid Aminotransferase. G. Livesey and P. Lund, Isolation and Characterization of Leucine Dehydrogenase from Bacillus subtilis. P.J. Sabourin and L.L. Bieber, Purification and Assay of ~ga-Ketoisocaproate Dioxygenase from Rat Liver. D.J. Danner and S.C. Heffelfinger, Isolation of Branched-Chain ~ga-Ketoacid Dehydrogenase as Active Complex from Bovine Liver. K.G. Cook and S.J. Yeaman, Purification, Resolution, and Reconstitution of Branched-Chain 2-Ketoacid Dehydrogenase Complex from Bovine Kidney. F.H. Pettit and L.J. Reed, Branched-Chain ~ga-Ketoacid Dehydrogenase Complex from Bovine Kidney. R. Paxton, Rabbit Liver and Heart Branched-Chain ~ga-Ketoacid Dehydrogenase and Its Kinase. Z. Damuni and L.J. Reed, Branched-Chain ~ga-Ketoacid Dehydrogenase Phosphatase and Its Inhibitor Protein from Bovine Kidney. R.N. Perham and P.N. Lowe, Isolation and Properties of the Branched-Chain 2-Ketoacid and Pyruvate Dehydrogenase Multienzyme Complex from Bacillus subtilis. J.R. Sokatch, Purification of Branched-Chain Ketoacid Dehydrogenase and Lipoamide Dehydrogenase-Valine from Pseudomonas. P.J. Sykes and J.R. Sokatch, Cloning of Genes for Branched-Chain Ketoacid Dehydrogenase in Pseudomonas Putida. Y. Ikeda and K. Tanaka, 2-Methyl Branched-Chain Acyl-CoA Dehydrogenase from Rat Liver. Y. Ikeda and K. Tanaka, Isovaleryl-CoA Dehydrogenase from Rat Liver. K. Hatter and J.R. Sokatch, Purification of Methylmalonate-Semialdehyde Dehydrogenase from Pseudomonas aeruginosa PAO. R.J. Kovachy, S.P. Stabler, and R.H. Allen, D-Methylmalonyl-CoA Hydrolase. S.P. Stabler and R.H. Allen, DL-Methylmalonyl-CoA Epimerase from Rat Liver. J.F. Kolhouse, S.P. Stabler, and R.H. Allen, L-Methylmalonyl-CoA Mutase from Human Placenta. G.B. Kohlhaw, ~ga-Isopropylmalate Synthase from Yeast. G.B. Kohlhaw, Isopropylmalate Dehydratase from Yeast. G.B. Kohlhaw, /-Isopropylmalate Dehydrogenase from Yeast. L. Eoyang and P.M. Silverman, Purification and Assays of Acetolactate Synthase I from Escherichia Coli K12. J.V. Schloss and D.E. Van Dyk, Acetolactate Synthase Isozyme II from Salmonella typhimurium. Z. Barak, J.M. Calvo, and J.V. Schloss, Acetolactate Synthase Isozyme III from Escherichia coli. Use of Animals and Animal Organs in the Study of Branched-Chain Amino Acid Metabolism. G.E. Mortimore and A.R. Pvsv, Amino Acid Control of Intracellular Protein Degradation. E.J. Davis, S.-H.C. Lee, ~alO. Spydevold, and J. Bremer, Use of Rat Hindquarter Preparations in Studies of Branched-Chain Amino Acid Metabolism. D.S. Lapointe, E. Hilderbrandt, D.B. Buxton, T.B. Patel, P.P. Waymack, and M.S. Olson, Measurement of Branched-Chain ~ga-Ketoacid Dehydrogenase Flux Rates in Perfused Heart and Liver. Index.

巻冊次

pt. B ISBN 9780121822255

内容説明

Volume 324 of Methods in Enzymology supplements Volume 166. It includes genetic information (cloning, gene expression) and information on human genetic diseases not available when Volume 166 was published.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.

目次

Section I: Preparation of Substrates, Assays of Intermediates and Enzymes, and Use of Enzyme Inhibitors [1]: Synthesis and Gas Chromatography/Mass Spectrometry Analysis of Stereoisomers of 2-Hydroxy-3-methylpentanoic Acid [2]: Analysis of Intracellular Metabolites as Tool for Studying Branched-Chain Amino Acid Biosynthesis and Its Inhibition in Bacteria [3]: Determination of Branched-Chain L-Amino-Acid Aminotransferase Activity [4]: Analysis of (S)- and (R)-3-Methyl-2-oxopentanoate Enantiomorphs in Body Fluids [5]: Spectrophotometric Assay for Measuring Branched-Chain Amino Acids [6]: Determination of Branched-Chain a-Keto Acid Dehydrogenase Activity State and Branched-Chain a-Keto Acid Dehydrogenase Kinase Activity and Protein in Mammalian Tissues [7]: Simultaneous Quantification of Plasma Levels of a-Ketoisocaproate and Leucine by Gas Chromatography-Mass Spectrometry [8]: Synthesis of Methacrylyl-CoA and (R)- and (S)-3-Hydroxyisobutyryl-CoA [9]: Pathways of Leucine and Valine Catabolism in Yeast Section II: Cloning, Expression, and Purification of Enzymes of Branched-Chain Amino Acid Metabolism [10]: Isolation of Subunits of Acetohydroxy Acid Synthase Isozyme III and Reconstitution of Holoenzyme [11]: Branched-Chain Amino-Acid Aminotransferase of Escherichia coli [12]: Purification of Sodium-Coupled Branched-Chain Amino Acid Carrier of Pseudomonas aeruginosa [13]: Reconstitution of Pseudomonas aeruginosa High-Affinity Branched-Chain Amino Acid Transport System [14]: Purification of Pseudomonas putida Branched-Chain Keto Acid Dehydrogenase E1 Component [15]: Pseudomonas mevalonii 3-Hydroxy-3-methylglutaryl-CoA Lyase [16]: Human 3-Hydroxy-3-methylglutaryl-CoA Lyase [17]: Branched-Chain a-Keto Acid Dehydrogenase Kinase [18]: Expression of E1 Component of Human Branched-Chain a-Keto Acid Dehydrogenase Complex in Escherichia coli by Cotransformation with Chaperonins GroEL GroES [19]: Production of Recombinant Mammalian Holo-E2 and E3 and Reconstitution of Functional Branched-Chain a-Keto Acid Dehydrogenase Complex with Recombinant E1 [20]: Production of Recombinant E1 Component of Branched-Chain a-Keto Acid Dehydrogenase Complex [21]: Mammalian Methylmalonate-Semialdehyde Dehydrogenase [22]: Mammalian 3-Hydroxyisobutyrate Dehydrogenase [23]: 3-Hydroxyisobutyryl-CoA Hydrolase [24]: Mammalian Branched-Chain Acyl-CoA Dehydrogenases: Molecular Cloning and Characterization of Recombinant Enzymes [25]: 3-Hydroxy-3-methylglutaryl-CoA Reductase [26]: Characterization of 3-Methylcrotonyl-CoA Carboxylase from Plants [27]: Purification of D-Hydroxyisovalerate Dehydrogenase from Fusarium sambucinum [28]: Purification and Characterization of Recombinant 3-Isopropylmalate Dehydrogenases from Thermus thermophilus Other Microorganisms [29]: Wild-Type and Hexahistidine-Tagged Derivatives of Leucine-Responsive Regulatory Protein from Escherichia coli [30]: Purification of Branched-Chain Keto Acid Dehydrogenase Regulator from Pseudomonas putida [31]: Mitochondrial Import of Mammalian Branched-Chain a-Keto Acid Dehydrogenase Complex Subunits [32]: Cloning, Expression, and Purification of Mammalian 4-Hydroxyphenylpyruvate Dioxygenase/a-Ketoisocaproate Dioxygenase [33]: Mammalian Branched-Chain Aminotransferases [34]: Branched-Chain-Amino-Acid Transaminases of Yeast Saccharomyces cerevisiae [35]: Purification, Properties, and Sequencing of Aminoisobutyrate Aminotransferases from Rat Liver [36]: Branched-Chain Keto Acid Dehydrogenase of Yeast [37]: ss-Alanine Synthase an Enzyme Involved in Catabolism of Uracil and Thymine Section III: Detection and Consequences of Genetic Defects in Genes Encoding Enzymes of Branched-Chain Amino Acid Metabolism [38]: Diagnosis and Mutational Analysis of Maple Syrup Urine Disease Using Cell Cultures [39]: Detection of Gene Defects in Branched-Chain Amino Acid Metabolism by Tandem Mass Spectrometry of Carnitine Esters Produced by Cultured Fibroblasts [40]: Molecular and Enzymatic Methods for Detection of Genetic Defects in Distal Pathways of Branched-Chain Amino Acid Metabolism [41]: Genetic Defects in E3 Component of a-Keto Acid Dehydrogenase Complexes [42]: Targeting E3 Component of a-Keto Acid Dehydrogenase Complexes Section IV: Regulation and Expression of Enzymes of Branched-Chain Amino Acid Metabolism [43]: Regulation of Expression of Branched-Chain a-Keto Acid Dehydrogenase Subunits in Permanent Cell Lines [44]: Expression of Murine Branched-Chain a-Keto Acid Dehydrogenase Kinase [45]: Regulation of Branched-Chain a-Keto Acid Dehydrogenase Kinase Gene Expression by Glucocorticoids in Hepatoma Cells and Rat Liver Author Index Subject Index

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詳細情報

• NII書誌ID(NCID): BA04998646
• ISBN:
  • 012182067X
  • 0121822257
• LCCN: 54009110
• 出版国コード: us
• タイトル言語コード: eng
• 本文言語コード: eng
• 出版地: San Diego ; Tokyo
• ページ数/冊数: 2 v.
• 大きさ: 24 cm
• 分類:
  • NLM : W1
• 件名:
  • MESH : Amino Acids, Branched-Chain
  • MESH : Keto Acids
• 親書誌ID:
  • BA00197543