Regulation of thermal stability of enzymes by changing the composition of media. Native and modified alpha-chymotrypsin
Levitskiĭ, V.I.; Melik-Nubarov, N.S.; Slepnev, V.I.; Shikshnis, V.A.; Mozhaev, V.V.
Molekuliarnaia Biologiia 24(5): 1246-1254
1990
ISSN/ISBN: 0026-8984 PMID: 2290421 Document Number: 349466
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.