Enzyme kinetics and mechanism / edited by Daniel L. Purich.
Series: Methods in enzymology ; v. 63-64, 87, 249, 308Publication details: New York : Academic Press, 1979-<1999 >Description: v. <pt. A-E > : ill. ; 24 cmISBN:- 0121819639 (pt. A)
- 0121819876 (pt. C)
- 0121821501 (pt. D)
- 0121822095 (pt. E)
- QU135 M592 1982 VOL.87
Item type | Current library | Call number | Copy number | Status | Date due | Barcode |
---|---|---|---|---|---|---|
Book Open Access | Health Sciences Library | QU135 M592 1982 VOL.87 (Browse shelf(Opens below)) | 1 | Available | MBAL22020371 |
Includes bibliographical references and indexes.
Contents
General Approaches to Biological Catalysis:
C.A. Fierke and G.G. Hammes, Transient Kinetic Approaches to Enzyme Mechanisms.
K.A. Johnson, Rapid Quench Kinetic Analysis of Polymerases, Adenosinetriphosphatases, and Enzyme Intermediates.
R.G. Duggleby, Analysis of Enzyme Progress Curves by Nonlinear Regression.
B.V. Plapp, Site-Directed Mutagenesis: A Tool for Studying Enzyme Catalysis.
Inhibitors as Mechanistic Probes:
H.J. Fromm, Reversible Enzyme Inhibitors as Mechanistic Probes.
S.E. Szedlacsek and R.G. Duggleby, Kinetics of Slow and Tight-Binding Inhibitors.
W.W. Cleland, Kinetic Method for Determination of Dissociation Constants of Metal Ion(Nucleotide Complexes.
B.F.Cooper and F.B. Rudolph, Product Inhibition Applications.
K.L. Rebholz and D.B. Northrop, Kinetics of Iso Mechanisms.
R.B. Silverman, Mechanism-Based Enzyme Inactivators.
A. Radzicka and R. Wolfenden, Transition State and Multisubstrate Analog Inhibitors.
Isotopic Probles of Enzyme Action:
I.A. Rose, Partition Analysis: Detecting Enzyme Reaction Cycle Intermediates.
W.W. Cleland, Isotope Effects: Determination of Enzyme Transition State Structure.
B.J. Bahnson and J.P. Klinman, Hydrogen Tunneling in Enzyme Catalysis.
L.S. Mullins and F.M. Raushel, Positional Isotope Exchange as Probe of Enzyme Action.
M.-D. Tsai, R.-T. Jiang, T. Dahnke, and Z. Shi, Manipulating Phosphorus Stereospecificity of Adenylate Kinase by Site-Directed Mutagenesis.
F.C. Wedler, Equilibrium Isotope Exchange in Enzyme Catalysis.
D.N. Silverman, Proton Transfer in Carbonic Anhydrase Measured by Equilibrium Isotope Exchange.
Kinetics of Specialized Systems:
J.D. Stewart, I. Lee, B.A. Posner, and S.J. Benkovic, Expression of Properly Folded Catalytic Antibodies in Escherichia coli.
K.E. Neet, Cooperativity in Enzyme Function: Equilibrium and Kinetic Aspects.
M.K. Jain, M.H. Gelb, J. Rogers, and O.G. Berg, Kinetic Basis for Interfacial Catalysis by Phospholipase A2.
Author Index.
pt. A. Initial rate and inhibitor methods -- pt. B. Isotopic probes and complex enzyme systems -- pt. C. Intermediates, stereochemistry, and rate studies -- pt. D. Developments in enzyme dynamics -- pt. E. Energetics of enzyme catalysis / edited by Vern L. Schramm, Daniel L. Purich.
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