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Steady-state kinetic study of action of ribonuclease A, involving a conformational change between 30 and 40 degrees C.

作者信息

Matheson R R, Scheraga H A

出版信息

Biochemistry. 1979 Jun 12;18(12):2446-50. doi: 10.1021/bi00579a002.

DOI:10.1021/bi00579a002
PMID:571735
Abstract

The steady-state kinetics of the reaction of ribonuclease A with cyclic cytidine 2',3'-phosphate as substrate are investigated as a function of temperature at pH 5 and ionic strength 0.1 M. The results suggest, but cannot prove, that a conformational change near 32 degrees C is involved in the rate-limiting step of the reaction mechanism. This conformational change is proposed to be the same one that was observed in studies of the free enzyme and of enzyme-inhibitor complexes near the same temperature.

摘要

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