Branched-Chain Amino Acids, Part B

Author:   John N. Abelson (California Institute of Technology, Division of Biology, Pasadena, U.S.A.) ,  Melvin I. Simon (The Salk Institute, La Jolla, CA, USA) ,  John R. Sokatch (University of Texas, Austin, U.S.A.) ,  Robert Adron Harris (University of Texas, Austin, U.S.A.)
Publisher:   Elsevier Science Publishing Co Inc
Volume:   324
ISBN:  

9780121822255


Pages:   550
Publication Date:   06 September 2000
Format:   Hardback
Availability:   In Print   Availability explained
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Branched-Chain Amino Acids, Part B


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Author:   John N. Abelson (California Institute of Technology, Division of Biology, Pasadena, U.S.A.) ,  Melvin I. Simon (The Salk Institute, La Jolla, CA, USA) ,  John R. Sokatch (University of Texas, Austin, U.S.A.) ,  Robert Adron Harris (University of Texas, Austin, U.S.A.)
Publisher:   Elsevier Science Publishing Co Inc
Imprint:   Academic Press Inc
Volume:   324
Dimensions:   Width: 15.20cm , Height: 3.60cm , Length: 22.90cm
Weight:   0.920kg
ISBN:  

9780121822255


ISBN 10:   0121822257
Pages:   550
Publication Date:   06 September 2000
Audience:   Professional and scholarly ,  Professional & Vocational
Format:   Hardback
Publisher's Status:   Out of Print
Availability:   In Print   Availability explained
Limited stock is available. It will be ordered for you and shipped pending supplier's limited stock.

Table of Contents

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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Praise for the Series The Methods in Enzymology series represents the gold-standard. --NEUROSCIENCE Incomparably useful. --ANALYTICAL BIOCHEMISTRY 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. --BIO/TECHNOLOGY 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. --CHEMISTRY IN INDUSTRY 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. --AMERICAN SOCIETY OF MICROBIOLOGY NEWS 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. --ENZYMOLOGIA A series that has established itself as a definitive reference for biochemists. --JOURNAL OF CHROMATOGRAPHY


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