Atypical serum creatine kinase isoenzyme pattern caused by complexing of creatine kinase-BB with immunoglobulins G and A1),2).
12 cases are described, which show high serum creatine kinase-BB levels, as well as atypical creatine kinase activity band located between normally migrating creatine kinase-MM and creatine kinase-MB. It is shown that the altered properties of the serum creatine kinase-BB, namely its molecular size, heat resistance, electrophoretic mobility, but not its immunological behavior, are caused by complexing with kappa-chains of immunoglobulins G or A. The complex occurring in vivo could also be produced in vitro by using purified patients' IgG and human creatine kinase-BB.
D000328:Adult; D000368:Aged; D001921:Brain / Q000201:enzymology; D003402:Creatine Kinase / Q000378:metabolism*; D005260:Female; D006801:Humans; D007070:Immunoglobulin A; D007074:Immunoglobulin G; D007527:Isoenzymes; D008297:Male; D008875:Middle Aged; D009132:Muscles / Q000201:enzymology; D011485:Protein Binding
D007070:Immunoglobulin A; D007074:Immunoglobulin G; D007527:Isoenzymes; D003402:Creatine Kinase