[Regulation of thermal stability of enzymes by changing the composition of media. Native and modified alpha-chymotrypsin].
作者信息
Levitskiĭ V Iu, Melik-Nubarov N S, Slepnev V I, Shikshnis V A, Mozhaev V V
出版信息
Mol Biol (Mosk). 1990 Sep-Oct;24(5):1246-54.
PMID:2290421
Abstract
Stabilizing effect of denaturing salts on irreversible thermoinactivation of native and modified alpha-chymotrypsin at elevated temperatures is observed. The effect is caused by a shift of conformational equilibrium, at the primary step of reversible unfolding in the course of thermoinactivation, to a more unfolded form which is not able to refold "incorrectly". The stability of alpha-chymotrypsin is regulated within a wide range by medium alteration: the stabilizing effects are similar to those achieved by multipoint attachment of the enzyme to a support or by hydrophilization of protein by covalent modification.
摘要
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