Rapid loss of lactate dehydrogenase isoenzyme activity in serum by cold-induced formation of immunoglobulin G-lactate dehydrogenase complex.

Abstract

Abstract Lactate dehydrogenase (LD; EC 1.1.1.27) activity in serum from a patient recovering from a myocardial infarction was extremely unstable when stored at 0 degree C. The activity of each LD isoenzyme except LD-1 decreased by at least 40% when serum was stored at 0 degree C for 4 h. The patient's erythrocyte LD activity had normal stability at lower temperatures, but LD from other sources, when added to the patient's serum, rapidly lost activity at 0 degree C. The patient's serum contained an immunoglobulin G that combined--at 0 degree C but not at 21 degrees C--primarily with LD isoenzymes containing one or more M subunits. Because this immunoglobulin-LD complex has no enzyme activity, we used 125I-labeled purified LD to study formation of the complex. NAD+ blocked the formation of immunoglobulin-LD complex but could not dissociate the complex and restore the LD activity.