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Heterogeneity of serum creatine kinase isoenzyme‐MM in acute myocardial infarction
Author(s) -
Williams John,
Williams Katherine M.,
Märshall Thomas
Publication year - 1989
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150100808
Subject(s) - creatine kinase , myocardial infarction , isozyme , cardiology , medicine , creatine , chemistry , biochemistry , enzyme
Isoelectric focusing of serum creatine kinase (CK; EC 2.7.3.2) reveals up to 14 CK‐MM subbands following acute myocardial infarction (AMI). The “normal” subbands 1 (p I 6.91), 2 (p I 6.65) and 3 (p I 6.35) are faintly present in normal serum and the “abnormal” subbands c (p I 7.25), e (p I 6.85), g (p I 6.50), i (p I 6.28), j (p I 6.20) and k (p I 6.15) are prominently detected in sera with elevated CK. “Abnormal” subbands a (p I 7.55), b (p I 7.35), d (p I 7.05), f (p I 6.72) and h (p I 6.40) have only been detected in AMI. The “abnormal” subbands appear, and reach maximum intensity (together with CK‐MM 1–3), 3–12 h after infarction, and become faint and anodally convert (as do CK‐MM 1–3) within 36 h. Similar changes are detected by nonequilibrium pH gradient electrophoresis which combines CK‐MM and CK‐MB analysis. In vitro incubation of serum with 0.015 M 2‐mercaptoethanol induces conversion of CK‐MM 1, 2 and 3 to b and c, d and e, and f and g, respectively. Thus, the complexity of the patterns is explained by a secondary conversion of “normal” to “abnormal” subbands superimposed upon anodal conversion of CK‐MM 1 → 3. The clinical significance of these findings is discussed.