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Low lactate dehydrogenase (LD; EC 1.1.1.27) activity and an abnormal LD pattern in electrophoretograms of LD isoenzymes in the sera of two patients were caused by inhibition of LD by immunoglobulin G. One of these showed inhibitor activity in the serum upon direct analysis, while the other showed activity only after the immunoglobulin was stripped from the LD. As judged from the LD isoenzyme patterns in serum, the LD inhibitor appeared to act against M subunits. However, quantification of binding affinities to each isolated isoenzyme showed that the LD inhibitor had a stronger effect on LD isoenzymes 2 and 3 (H3M1 and H2M2, respectively).
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