|
Volumn 6, Issue 1-2, 1999, Pages 11-20
|
α-chymotrypsin stability in aqueous-acetonitrile mixtures: Is the native enzyme thermodynamically or kinetically stable under low water conditions?
|
Author keywords
Chymotrypsin; Aqueous acetonitrile mixtures; Enzyme denaturation renaturation; Kinetic stability; Organic solvent
|
Indexed keywords
ACETONITRILE;
CATALYSIS;
CATALYST ACTIVITY;
COMPOSITION EFFECTS;
ENZYME KINETICS;
ORGANIC SOLVENTS;
THERMAL EFFECTS;
THERMODYNAMIC STABILITY;
WATER;
CHYMOTRYPSIN;
ENZYME DENATURATION/RENATURATION;
ENZYMES;
ACETONITRILE;
CHYMOTRYPSIN A;
ORGANIC SOLVENT;
AQUEOUS SOLUTION;
ARTICLE;
CATALYSIS;
CONFORMATIONAL TRANSITION;
ENZYME DENATURATION;
ENZYME INACTIVATION;
ENZYME KINETICS;
ENZYME STABILITY;
HYDROGEN BOND;
PROTEIN SECONDARY STRUCTURE;
PROTEIN STABILITY;
|
EID: 0033521506
PISSN: 13811177
EISSN: None
Source Type: Journal
DOI: 10.1016/S1381-1177(98)00105-2 Document Type: Article |
Times cited : (31)
|
References (23)
|