Wicking C A, Scholem R D, Hunt S M, Brown G K
Biochem J. 1986 Oct 1;239(1):89-96. doi: 10.1042/bj2390089.
Pyruvate dehydrogenase (PDH) deficiency has been described in many patients with primary lactic acidosis. However, there are very few cases in which a structural defect in the complex has been clearly demonstrated. Measurement of the activity of the PDH complex in cultured human cells has proved unreliable, and a combination of structural and functional studies are required to make a definitive diagnosis. For this reason, an immunochemical strategy has been developed to complement direct enzyme assay in the detection and further characterization of PDH deficiency. We illustrate the usefulness of this approach by describing defects in the alpha-subunit of the pyruvate decarboxylase component of the PDH complex in two patients with primary lactic acidosis. In one patient, there is no immunologically cross-reacting material corresponding to this subunit. In the second patient, there appears to be an intrinsic structural defect in the subunit which restricts dephosphorylation (and hence activation) of the inactive phosphorylated complex.
丙酮酸脱氢酶（PDH）缺乏症在许多原发性乳酸性酸中毒患者中已有报道。然而，复合物存在结构缺陷的明确病例非常少见。在培养的人类细胞中测量PDH复合物的活性已被证明不可靠，需要结合结构和功能研究才能做出明确诊断。因此，已开发出一种免疫化学策略，以补充直接酶测定法，用于检测和进一步表征PDH缺乏症。我们通过描述两名原发性乳酸性酸中毒患者中PDH复合物丙酮酸脱羧酶成分α亚基的缺陷，来说明这种方法的实用性。在一名患者中，没有与该亚基相对应的免疫交叉反应物质。在第二名患者中，该亚基似乎存在内在结构缺陷，限制了无活性磷酸化复合物的去磷酸化（从而激活）。
