Why the study?
Does an immunoinhibition assay using monoclonal antibody CKM-G01 accurately quantify creatine kinase isoforms compared to the electrophoretic method?
Does an immunoinhibition assay using monoclonal antibody CKM-G01 accurately quantify creatine kinase isoforms compared to the electrophoretic method?
The immunoinhibition assay using monoclonal antibody CKM-G01 is a viable alternative to electrophoresis for measuring the creatine kinase isoform ratio.
Supports immunoinhibition assay as potential alternative for CK isoform measurement; leaves open need for larger validation before routine use.
We report a preliminary evaluation of an immunoinhibition assay for creatine kinase isoform quantification. The procedure employs the monoclonal antibody CKM-G01, which inhibits the native M subunit of creatine kinase. The antibody does not inhibit the M subunit modified by removal of lysine by plasma carboxypeptidase N. Residual activity after treatment with the antibody is therefore due to serum delysinated isoforms. The ratio inhibited/residual activity correlated directly with the ratio tissue/serum isoforms. Analysis of the total imprecision of isoform ratio measurement gave a coefficient of variation between 5.9 and 21.1%. Reference intervals for the ratio were 0.14-0.79 in females and 0.19-0.95 in men (p = 0.0046). Analytical and clinical comparison with alternative isoform procedures gave good results, showing that this assay can be used as alternative to the widely accepted electrophoretic method for measurement of the creatine kinase isoform ratio.
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Panteghini et al. (1994) studied this question.
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