Kinetic Properties of the Isoenzymes of Human Creatine Phosphokinase | Zendy

S. A. G. J. Witteveen | Zendy; Burton E. Sobel | Zendy; M. DeLuca | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Kinetic Properties of the Isoenzymes of Human Creatine Phosphokinase

Author(s) -

S. A. G. J. Witteveen,

Burton E. Sobel,

M. DeLuca

Publication year - 1974

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.71.4.1384

Subject(s) - isozyme , creatine kinase , substrate (aquarium) , firefly protocol , biochemistry , luciferase , enzyme , chemistry , biology , medicine , gene , ecology , zoology , transfection

Studies of the three human creatine phosphokinase (EC 2.7.3.2) isoenzymes, MM, MB, and BB, show that important differences exist in substrate dependency of the reaction rates. A method was developed to study these properties in which the ATP formed in the reverse reaction was measured by means of firefly luciferase. With substrate conditions at which the isoenzymes showed substantial differences in activity the method could be used for the detection of changes in the isoenzyme pattern of the serum of patients with an acute myocardial infarction. The MB isoenzyme appearing in this condition could be detected quantitatively.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research