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Annals of Clinical & Laboratory Science 36:461-468 (2006)
© 2006 Association of Clinical Scientists

An Immunoglobulin A1 that Inhibits Lactate Dehydrogenase Activity, with Reversal of Inhibition by Addition of NADH

Kiyotaka Fujita1, Hirohisa Sato2, Fumiko Kameko1, Fumiko Terasawa1, Nobuo Okumura1, Mitsutoshi Sugano3, Kazuyoshi Yamauchi3, Masato Maekawa4 and Ikunosuke Sakurabayashi5
1 Department of Biomedical Laboratory Sciences, School of Health Sciences, Shinshu University, Matsumoto; 2 Department of Clinical Laboratories, Aomori Prefectural Central Hospital, Aomori; 3 Department of Laboratory Medicine, Shinshu University School of Medicine, Matsumoto; 4 Department of Laboratory Medicine, Hamamatsu University School of Medicine, Hamamatsu; and 5 Department of Clinical Laboratories, Omiya Medical Center, Jichi Medical School, Saitama, Japan

Address correspondence to Kiyotaka Fujita, Ph.D., Department of Biomedical Laboratory Sciences, School of Health Sciences, Shinshu University, 3-1-1 Asahi, Matsumoto, Nagano, 390-8621, Japan; tel & fax: 81 263 37 2390; e-mail address: kyfujit{at}gipac.shinshu-u.ac.jp.

We discovered a patient with low serum lactate dehydrogenase (LD) activity and an abnormal LD isozyme pattern. We analyzed the patient’s LD inhibitor using electrophoresis, affinity chromatography, and immunochemical technologies. The LD activity of the patient’s serum was inhibited more strongly at 4°C than at 37°C. The decrease of LD activity was more marked in a mixture of the patient’s serum with purified LD5 than in that with purified LD1. The immunoglobulin responsible for LD inhibition was an IgA1-{lambda}. The LD inhibition by the patient’s IgA1 was blocked by reduction and alkylation and by NADH. Polymerization of the patient’s IgA1 might play an important role in its interaction with LD. Moreover, the possibility exists that part of the patient’s IgA1 molecule fits into a pocket of LD in instead of NADH. This is the first report of NADH reversing such LD inhibition.

Keywords: lactate dehydrogenase, LD isozyme anomaly, LD-IgA1 complexes, NAD+-binding site






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