The creatine kinase molecule is a dimer consisting of a brain-type subunit (B) and a muscle-type subunit (M). Normal human tissues often contain 3 isoenzymes, which are CK-BB (CK1), CK-MB (CK2) and CK-MM (CK3) in the order of electrophoresis. CK-BB mainly exists in smooth muscle and brain tissue, and almost no serum; CK-MB mainly exists in myocardial tissue, accounting for 0-4% of CK in serum; CK-MM mainly exists in skeletal muscle, accounting for 0% of serum CK-MM. 96% to 100% of CK. CK-MB has its own subtypes, including MB2 (organized form) and MB1 (transformed form). After CK-MB2 is released from the myocardium, the carboxyl terminus is hydrolyzed by plasma carboxypeptidase N, which removes a lysine residue and converts it to the serum-modified isoform CK-MB1. CK and CK-MB are one of the sensitive indicators of myocardial tissue damage, especially CK-MB is more specific. The increase of CK in the process of myocardial injury is mainly caused by the increase of CK-MB, which is manifested as the simultaneous increase of both.
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