Fujita K, Takeya C, Saito T, Sakurabayashi I
Clin Chim Acta. 1984 Jul 16;140(2):183-95. doi: 10.1016/0009-8981(84)90343-7.
A macro lactate dehydrogenase (LDH, EC 1.1.1.27) isoenzyme with a low total LDH activity was present in the serum of a 57-year-old woman with a drug eruption (cutaneous lesions from an allergic reaction to drug administration). The patient's LDH was shown by immunoelectrophoresis to be bound to immunoglobulin G (IgG) and M (IgM). It was found that the patient's IgM acted as an inhibitor of LDH that was specific for the M subunit. When IgM was treated with 0.1 mol/l of 2-mercaptoethanol (2-ME), the inhibiting effect of the IgM to LDH activity disappeared, while treated IgM continued to bind to the LDH molecule. The LDH activity increased approximately two-fold when the patient's serum was treated with 2-ME. LDH activity in normal human serum was inhibited and an abnormal pattern of LDH isoenzyme appeared when the patient's IgM was added to normal serum. The present case seems to be the first report of LDH-IgM complex with a marked decrease of LDH activity.
一名57岁患有药疹(药物给药过敏反应引起的皮肤病变)的女性血清中存在一种总乳酸脱氢酶(LDH,EC 1.1.1.27)活性较低的宏观乳酸脱氢酶同工酶。免疫电泳显示患者的LDH与免疫球蛋白G(IgG)和M(IgM)结合。发现患者的IgM作为对M亚基具有特异性的LDH抑制剂。当用0.1mol/L的2-巯基乙醇(2-ME)处理IgM时,IgM对LDH活性的抑制作用消失,而处理后的IgM继续与LDH分子结合。用2-ME处理患者血清时,LDH活性增加约两倍。当将患者的IgM添加到正常人血清中时,正常人血清中的LDH活性受到抑制,并且出现异常的LDH同工酶模式。本病例似乎是LDH活性显著降低的LDH-IgM复合物的首次报道。