Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems
Covers enzyme kinetics from its most elementary aspects to such modern subjects as steady-state, multi-reactant kinetics and isotope exchange. Offers an understanding of the behavior of enzyme systems and the diagnostic tools used to characterize them and determine kinetic mechanisms. Illustrates and explains current subjects such as cumulative, concerted and cooperative feedback inhibition and metal ion activation.
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1/v versus 1/v-axis intercept activator affinity apparent assay assumed axis becomes binding Biochem calculated catalytic Chapter combine competitive inhibitor complex conformation constant containing cooperativity corresponding decreases denominator derived described determined different fixed dissociation constant effect enzyme equal example exclusive expressed factor fixed concentrations four fraction given gives Hill hyperbolic identical increases inhibition initial velocity interaction factors intercept intersect kinetic ligand limiting linear max max mixed-type molecule multiplied noncompetitive inhibition observed obtained occupied Ordered partial presence protein pure Random range Rapid Equilibrium rate constants ratio reaction reciprocal plot relative replot represents respect result saturating shown shown in Figure shows sigmoidal slope specific substrate binding substrate concentration subunit tion true usual values varied velocity curve velocity equation versus Vmax yield
Quantitative Aspects of Ruminant Digestion and Metabolism
J. Dijkstra,J. M. Forbes,J. France
No preview available - 2005
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Progress in Nucleic Acid Research and Molecular Biology, Volume 59
Limited preview - 1998