Clinical Chemistry, Vol 35, 206-210, Copyright © 1989 by American Association for Clinical Chemistry

Heterogeneity of serum creatine kinase isoenzyme MM in myocardial infarction: clinical significance and post-synthetic conversion of "abnormal" sub-bands

J Williams, KM Williams and T Marshall
Biochemistry Department, General Hospital, Sligo, Ireland.

We investigated the "abnormal" sub-bands of serum creatine kinase (CK; EC 2.7.3.2) isoenzyme MM in acute myocardial infarction (AMI), using isoelectric focusing in polyacrylamide gels, and compared the patterns with those for non-AMI patients and for athletes with increased CK. The "abnormal" sub-bands a (pI 7.55), b (pI 7.35), c (pI 7.25), d (pI 7.05), e (pI 6.85), f (pI 6.72), g (pI 6.50), h (pI 6.40), i (pI 6.28), j (pI 6.20), and k (pI 6.15), in common with "normal" sub-bands 1 (pI 6.91), 2 (pI 6.65), and 3 (pI 6.35), were less uniformly distributed in the AMI and demonstrated a faster rate of anodal conversion than in the non-AMI patients and athletes. "Abnormal" sub-bands a and b were detected only in the AMI patients. Incubation of myocardial CK-MM, predominantly CK-MM 1, with 2-mercaptoethanol, 15 mmol/L, resulted in conversion to the "abnormal" sub-bands b and c. Incubation of myocardial CK-MM with normal serum of low total CK yielded CK-MM 3, which on further incubation with 2-mercaptoethanol, 15 mmol/L, resulted in conversion to the "abnormal" sub-bands f and g. Comparable in vitro incubation of serum from AMI patients gave pattern changes consistent with conversion of CK-MM 1 to b, c; CK-MM 2 to d, e; and CK-MM 3 to f, g.