Branched-Chain Amino Acids, Part B: Volume 324

Branched-Chain Amino Acids, Part B: Volume 324

Editor-in-chief  , Editor-in-chief  , Volume editor  , Volume editor 

Free delivery worldwide

Available. Dispatched from the UK in 2 business days
When will my order arrive?


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.
show more

Product details

  • Hardback | 550 pages
  • 159 x 235.5 x 31.8mm | 995.29g
  • Academic Press Inc
  • San Diego, United States
  • English
  • 0121822257
  • 9780121822255

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 -Keto Acid Dehydrogenase Activity State and Branched-Chain -Keto Acid Dehydrogenase Kinase Activity and Protein in Mammalian Tissues

[7]: Simultaneous Quantification of Plasma Levels of -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 -Keto Acid Dehydrogenase Kinase

[18]: Expression of E1 Component of Human Branched-Chain -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 -Keto Acid Dehydrogenase Complex with Recombinant E1

[20]: Production of Recombinant E1 Component of Branched-Chain -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 -Keto Acid Dehydrogenase Complex Subunits

[32]: Cloning, Expression, and Purification of Mammalian 4-Hydroxyphenylpyruvate Dioxygenase/ -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 -Keto Acid Dehydrogenase Complexes

[42]: Targeting E3 Component of -Keto Acid Dehydrogenase Complexes

Section IV: Regulation and Expression of Enzymes of Branched-Chain Amino Acid Metabolism

[43]: Regulation of Expression of Branched-Chain -Keto Acid Dehydrogenase Subunits in Permanent Cell Lines

[44]: Expression of Murine Branched-Chain -Keto Acid Dehydrogenase Kinase

[45]: Regulation of Branched-Chain -Keto Acid Dehydrogenase Kinase Gene Expression by Glucocorticoids in Hepatoma Cells and Rat Liver

Author Index

Subject Index
show more

Review quote

Praise for the Series
"The Methods in Enzymology series represents the gold-standard."
"Incomparably useful."
"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."
"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."
"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."
"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."
"A series that has established itself as a definitive reference for biochemists."
show more