A new creatine kinase found in mitochondrial extracts from malignant liver tissue.
A new creatine kinase (CK, ATP: creatine N-phosphotransferase, EC 2.7.3.2) band was found in mitochondrial extracts prepared from malignant liver tissue. By agar gel electrophoresis the new band (CKmLT) migrated between CK-MM and a sample application point. The CK band was not found in mitochondrial extracts of normal liver, cytosolic extracts of normal and malignant liver homogenates. We thus presume that the origin of CKmLT is from mitochondria of malignant liver tumors. CKmLT reacted with anti-mitochondrial CK antibodies so that its antigenicity was similar to that of mitochondrial CK. Physico-chemical characteristics were similar to those of the polymeric form of the normal liver mitochondrial CK (CKmL1); i.e. relative molecular mass (320 000 to 350 000), heat stability, and the behavior in 2 mol/l urea. CKmLT migrated to the CKmL1 and the MM position after long-term storage at -20 degrees C. CKmLT did not demonstrate affinity to concanavalin A, and there was no significant change in the electrophoretic mobility of CKmLT following neuraminidase treatment.
D000328:Adult; D002846:Chromatography, Affinity; D003402:Creatine Kinase / Q000097:blood / Q000378:metabolism*; D004587:Electrophoresis, Agar Gel; D005260:Female; D006801:Humans; D007158:Immunologic Techniques; D007527:Isoenzymes; D008113:Liver Neoplasms / Q000201:enzymology*; D008875:Middle Aged; D008930:Mitochondria, Liver / Q000201:enzymology*; D008970:Molecular Weight
D007527:Isoenzymes; D003402:Creatine Kinase