An approach to inhibition kinetics. Measurement of enzyme-substrate complexes by electronic energy transfer.
An approach to inhibition kinetics. Measurement of enzyme-substrate complexes by electronic energy transfer.
复制标题
抑制动力学的方法。
DOI：
10.1021/bi00776a019
复制
发表时间：
1972
期刊：
影响因子：
2.9
通讯作者：
B. Vallée
中科院分区：
文献类型：
--
作者：
D. Auld;S. Latt;B. Vallée
David S. Auld, Samuel A. Latt,+ and Bert L. Vallee* abstract: The rapidformation and breakdown of enzymesubstrate (ES) complexes between N-dansylated peptide sub-strates andcarboxypeptidase A can be followed by stopped-flow fluorescence. The maximal fluorescence and the decay of the signal can be related to Michaelis-Menten parameters. The maximal fluorescence, Fmax, is directly proportional to the steady state concentration of the ES complex, andthe area under the curve, A, is inversely proportional to the hydrolysis rate kV! Xt. Measurement of Fmax and values of A at different substrate concentrations allow determination of the kinetic parameters Kr, and A (at. The mode of action of an inhibitor can be identified directly bythe manner in which it
