Type

Journal Article

Authors

C Kilty
R O'Kennedy
H Sheehan

Subjects

Biochemistry

Topics
metabolism time factors creatine kinase cross linking reagents hot temperature pharmacology animals kinetics enzyme stability cattle thermodynamics myocardium protein denaturation enzymology dimethyl suberimidate

Investigation of the properties of bovine heart creatine kinase cross-linked with dimethyl suberimidate. (1990)

Abstract Dimeric bovine heart creatine kinase (EC 2.7.3.2, ATP: creatine N-phosphotransferase) has been cross-linked with the bifunctional reagent dimethyl suberimidate at several concentrations to yield modified enzyme with enhanced stability towards heat denaturation. The degree of thermal stability is dependent on the degree of cross-linking with optimal stabilization occurring when approx. half of all the available amino groups are covalently attached to dimethyl suberimidate. Accelerated storage studies were performed and the results used to predict the storage time of the native and modified enzyme at lower temperatures. The cross-linked derivative was predicted to have a longer shelf-life at 4 degrees C than the native enzyme. Modification caused a reduction in the specific activity of the enzyme. The pH profile was altered following cross-linking, but the Michaelis constants were not changed. The modified enzyme exhibited a marked resistance to the action of some denaturing agents.
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Full list of authors on original publication

C Kilty, R O'Kennedy, H Sheehan

Experts in our system

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R O'Kennedy
Dublin City University
Total Publications: 197