Creatine kinase isoenzymes of mitochondrial origin in human serum.
Open Access
- 1 June 1979
- journal article
- research article
- Published by Oxford University Press (OUP) in Clinical Chemistry
- Vol. 25 (6) , 943-947
- https://doi.org/10.1093/clinchem/25.6.943
Abstract
We measured creatine kinase (EC 2.7.3.2) activity in 1009 serum samples from 538 patients in the intensive-care units of the University of Texas Medical Branch hospitals. Creatine kinase isoenzymes migrating cathodal to skeletal muscle creatine kinase (CK-MM) on cellulose acetate electrophoresis were found in sera from 14 of the 538 patients. Creatine kinase, lactate dehydrogenase (EC 1.1.1.27), aspartate aminotransferase (EC 2.6.1.1), and alanine aminotransferase (EC 2.6.1.2) activities were abnormally increased in these 14 patients. Liver lactate dehydrogenase isoenzyme (LDH5) and cardiac creatine kinase isoenzyme (CK-MB) were abnormally increased in 12 and eight of these patients, respectively. Ten of the 14 patients died during their hospital admission. We believe the creatine kinase isoenzymes that migrated cathodal to skeletal muscle creatine kinase (CK-MM) were of mitochondrial origin.This publication has 3 references indexed in Scilit:
- Creatine kinase isoenzyme MB in myocardial infarction: methods compared.Clinical Chemistry, 1977
- The further heterogeneity of creatine kinaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1976
- High activity of creatine kinase in mitochondria from muscle and brain and evidence for a separate mitochondrial isoenzyme of creatine kinaseBiochemical and Biophysical Research Communications, 1964