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乳酸脱氢酶复合物的变异表达,干扰同工酶分析。

Variant expression of lactate dehydrogenase complexes, interfering with isoenzyme analysis.

作者信息

de Rijke D, Trienekens P H

出版信息

Clin Chim Acta. 1985 Mar 15;146(2-3):135-45. doi: 10.1016/0009-8981(85)90052-x.

Abstract

Three patients with an elevated serum LD activity and unusual, but quite different LD isoenzyme patterns, were studied. It was shown by immunofixation procedures, that complexes between LD isoenzymes and immunoglobulins of the IgG-kappa, IgA-kappa and IgG-lambda class, respectively, caused the observed isoenzyme patterns. From mixing experiments it appeared that the immunoglobulins were specific for either the H-subunit only or an antigenic determinant expressed by a combination of H- and M-subunits in the LD isoenzymes. The observed complexes could be dissociated, in vitro, with NAD+ in two patients, while in the third patient the complex was resistant to NAD+ addition. No common denominator was found with respect to clinical diagnosis. Auto-immune disorders or infection with hepatitis B virus were not involved.

摘要

对3例血清乳酸脱氢酶(LD)活性升高且具有异常但截然不同的LD同工酶谱的患者进行了研究。免疫固定法显示,分别由IgG-κ、IgA-κ和IgG-λ类免疫球蛋白与LD同工酶形成的复合物导致了观察到的同工酶谱。混合实验表明,这些免疫球蛋白仅对H亚基或由LD同工酶中H亚基和M亚基组合表达的抗原决定簇具有特异性。在两名患者中,观察到的复合物在体外可被NAD⁺解离,而在第三名患者中,该复合物对添加NAD⁺具有抗性。在临床诊断方面未发现共同特征。未涉及自身免疫性疾病或乙型肝炎病毒感染。

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