KINETIC-ANALYSIS OF A MICHAELIS-MENTEN MECHANISM IN WHICH THE ENZYME IS UNSTABLE

被引：16
|
作者：
GARRIDODELSOLO, C
GARCIACANOVAS, F
HAVSTEEN, BH
VARONCASTELLANOS, R
机构：
[1] UNIV MURCIA,FAC BIOL,DEPT BIOQUIM & BIOL MOLEC,E-30071 MURCIA,SPAIN
[2] CHRISTIAN ALBRECHTS UNIV KIEL,FAK MED,INST BIOCHEM,W-2300 KIEL 1,GERMANY
来源：
BIOCHEMICAL JOURNAL | 1993年 / 294卷
关键词：
D O I：
10.1042/bj2940459
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A kinetic analysis of the Michaelis-Menten mechanism is made for the cases in which the free enzyme, or the enzyme-substrate complex, or both, are unstable, either spontaneously or as a result of the addition of a reagent. The explicit time-course equations of all of the species involved has been derived under conditions of limiting enzyme concentration. The validity of these equations has been checked by using numerical simulations. An experimental design and a kinetic data analysis allowing the evaluation of the parameters and kinetic constants are recommended.
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收藏
页码：459 / 464
页数：6
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