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Clinical Chemistry 30: 11-17, 1984;
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Clinical Chemistry, Vol 30, 11-17, Copyright © 1984 by American Association for Clinical Chemistry

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

GG Wickus and MJ Smith

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.


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 Annals of Clinical & Laboratory ScienceHome page
K. Fujita, H. Sato, F. Kameko, F. Terasawa, N. Okumura, M. Sugano, K. Yamauchi, M. Maekawa, and I. Sakurabayashi
An Immunoglobulin A1 that Inhibits Lactate Dehydrogenase Activity, with Reversal of Inhibition by Addition of NADH
Ann. Clin. Lab. Sci., January 1, 2006; 36(4): 461 - 468.
[Abstract] [Full Text] [PDF]


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Copyright © 1984 by the American Association for Clinical Chemistry.