Effect of Triton X-100 on the electrophoretic mobility of the creatine kinase isoenzymes of serum and tissues.
The distribution of creatine kinase isoenzymes was studied in homogenates of human skeletal muscle, myocardium and brain tissue, and in sera. For the study of the cytosolar isoenzymes (MM, MB, BB) the tissues were homogenized with a Ca++- and Mg++-containing buffer. The membrane-associated isoenzymes were solubilized with buffer containing 1% Triton X-100. The isoenzymes were separated on polyacrylamide gel slabs. After treatment with Triton X-100 a membrane-associated isoenzyme of high activity, corresponding in mobility to cytosolar MM, was identified in brain tissue. No similar fraction was demonstrable in muscle tissue. The difference in the results is attributed to differences in the sensitivity of the creatine kinase isoenzymes of muscle and brain tissues. The cytosolar MM fraction of human sera is of more anodal mobility than that of tissue homogenates, and in the MM region subfractions have been demonstrated in some cases. Triton X-100 did not affect the electrophoretic mobility of the creatine kinase isoenzymes of the sera, or of the tissue homogenates.
D002540:Cerebral Cortex / Q000201:enzymology; D003402:Creatine Kinase / Q000097:blood*; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D006801:Humans; D007527:Isoenzymes; D009132:Muscles / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D017830:Octoxynol; D011092:Polyethylene Glycols / Q000494:pharmacology*
D007527:Isoenzymes; D011092:Polyethylene Glycols; D017830:Octoxynol; D003402:Creatine Kinase