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| ENZYME KINETICS AND MECHANISM, PART F: DETECTION AND CHARACTERIZATION OF ENZYME REACTION INTERMEDIATES, 354
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 Methods in Enzymology
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By
Daniel Purich, University of Florida, Gainesville, U.S.A.
Description
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.
Audience
Biochemists, biophysicists, pharmacologists, molecular biologists, analytical, organic, and medicinal chemists, and graduate students in these disciplines
Contents
Covalent Enzyme-Substrate Compounds: Detection and Catalytic Competence
Rapid Mix-Quench MALDI-TOF Mass Spectrometry for Analysis of Enzymatic
Systems
Pre-Steady-State Kinetics of Enzymatic Reactions Studied by Electrospray Mass Spectrometry with On-Line Rapid-Mixing Techniques
Trapping of -Glycosidase Intermediates
Trapping Covalent Intermediates on ?-Glycosidases
2-Hydroxy-6-keto-nona-2,4-diene 1,9-Dioic
Acid 5,6-Hydrolase: Evidence from18O Isotope Exchange for gem-Diol Intermediate
Nucleoside-Diphosphate Kinase: Structural and Kinetic
Analysis of Reaction Pathway and Phosphohistidine Intermediate
Galactose-1-Phosphate Uridylyltransferase: Kinetics of Formation and Reaction
of Uridylyl-Enzyme Intermediate in Wild-Type and Specifically Mutated Uridylyltransferases
Kinetic Evidence for Covalent Phosphoryl-Enzyme
Intermediate in Phosphotransferase Activity of Human Red Cell Pyrimidine Nucleotidases
Characterization of (2->6) -Sialyltransferase
Reaction Intermediates: Use of Alternative Substrates to Unmask Kinetic Isotope Effects
Use of Sodium Borohydride to Detect Acyl-Phosphate
Linkages in Enzyme Reactions
Evidence for Phosphotransferases Phosphorylated on Aspartate Residue in N-Terminal DXDX(T/V) Motif
MurC
and MurD Synthetases of Peptidoglycan Biosynthesis: Borohydride Trapping of Acyl-Phosphate Intermediates
Transaldolase B: Borohydride
Reduction Trapping of Schiff Base Intermediate between Dihydroxyacetone and -Amino Group of Active-Site Lysine Residue
Use of
NMR and Borohydride Trapping to Provide Evidence for Covalent Enzyme-Substrate Imine Intermediate
Detection of Covalent Tetrahedral Adducts
by Differential Isotope Shift ??C NMR: Acetyl-Enzyme Reaction Intermediate Formed by 3-Hydroxy-3-methylglutaryl-CoA Synthase
Detection
of Intermediates in Reactions Catalyzed by PLP-Dependent Enzymes: O-Acetylserine Sulfhydrylase and Serine-Glyoxalate Aminotransferase
Protein Tyrosine Phosphatase: X-Ray Crystallographic Observation of Cysteinyl-Phosphate Reaction Intermediate
GTP:GTP Guanylyltransferase:
Trapping Procedures for Detecting and Characterizing Chemical Nature of Enzyme-Nucleotide Phosphoramidate Reaction Intermediate-Glutamyl
Thioester Intermediate in Glutaminase Reaction Catalyzed by Escherichia coli Asparagine Synthetase B-Glutamyltranspeptidase
and -Glutamyl Peptide Ligases: Fluorophosphonate and Phosphonodifluoromethyl Ketone Analogs as Probes of Tetrahedral Transition
State and -Glutamyl-Phosphate Intermediate
Stoichiometric Redox Titrations of Complex Metalloenzymes
Urate Oxidase: Single-Turnover
Stopped-Flow Techniques for Detecting Two Discrete Enzyme-Bound Intermediates
Nitric Oxide Synthase: Use of Stopped-Flow Spectroscopy
and Rapid-Quench Methods in Single-Turnover Conditions to Examine Formation and Reactions of Heme- O2 Intermediate in Early Catalysis
Myeloperoxidase: Kinetic Evidence for Formation of Enzyme-Bound Chlorinating Intermediate
Time-Resolved Resonance Raman Spectroscopy
of Intermediates in Cytochrome Oxidase
Porphobilinogen Deaminase: Accumulation and Detection of Tetrapyrrole Intermediates Using Enzyme
Immobilization
Adenosylcobalamin-Dependent Glutamate Mutase: Pre-Steady-State Kinetic Methods for Investigating Reaction Mechanism
Ribonucleotide
Reductase: Kinetic Methods for Demonstrating Radical Transfer Pathway in Protein R2 of Mouse Enzyme in Generation of Tyrosyl Free Radical
Galactose Oxidase: Probing Radical Mechanism with Ultrafast Radical Probe
Kinetic Characterization of Transient Free Radical Intermediates
in Reaction of Lysine 2,3-Aminomutase by EPR Lineshape Analysis
Demonstration of Peroxodiferric Intermediate in M-Ferritin Ferroxidase
Reaction Using Rapid Freeze-Quench Mossbauer, Resonance Raman, and XAS Spectroscopies
A Survey of Covalent, Ionic, and Radical
Intermediates
in Enzyme-Catalyzed Reactions
| Bibliographic details |
Hardbound, 650 pages, publication date: OCT-2002
ISBN-13: 978-0-12-182257-6
ISBN-10: 0-12-182257-5
Imprint: ACADEMIC PRESS
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| Price and Ordering |
Price:
USD 175
GBP 88
EUR 128
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Last update: 8 Nov 2008
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