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PMID: 4524644 Published · ppublish English Journal Article

Kinetic properties of the isoenzymes of human creatine phosphokinase.

Witteveen SA, Sobel BE, DeLuca M

Abstract

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.

MeSH Terms
Adenosine Triphosphate/biosynthesis Creatine Kinase/blood,metabolism Diagnosis, Differential Humans Insecta Isoenzymes/blood,metabolism Kinetics Luciferases Luminescent Measurements Myocardial Infarction/blood,diagnosis,metabolism
Chemicals
Isoenzymes Adenosine Triphosphate Luciferases Creatine Kinase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Witteveen S A
Sobel B E
DeLuca M
References (18)
18 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1974-04-00
Pages
1384-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC388233
Subset
IM
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