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Clinical Chemistry 32: 1347-1349, 1986;
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Clinical Chemistry, Vol 32, 1347-1349, Copyright © 1986 by American Association for Clinical Chemistry

Lactate dehydrogenase inhibition by immunoglobulin G in human serum

M Maekawa, K Sudo, K Iwahara and T Kanno

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).


The following articles in journals at HighWire Press have cited this article:


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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.
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Copyright © 1986 by the American Association for Clinical Chemistry.