Department of Biological Chemistry, Hahnemann Medical College, 230 North Broad Street, Philadelphia, Pennsylvania, 19102, USA.
J Eukaryot Microbiol. 2021 May;68(3):e12851. doi: 10.1111/jeu.12851. Epub 2021 Apr 15.
An NAD-linked lactate dehydrogenase (LDH) in a crude mitochondrial fraction obtained from Tetrahymena homogenates was previously reported by this laboratory. This fraction contains the NADH and succinate oxidase system as well as the mitochondrial cytochromes and carries out oxidative phosphorylation. The preparation catalyzes the oxidation of D- and L-lactate linked only to certain analogs of NAD; it has not been possible to demonstrate NAD-dependent D- or L-lactate oxidation nor is there any evidence that either of these enzymes is a flavoprotein as indicated by their inability to reduce directly certain artificial electron acceptors. A lactate racemase is not present.
本实验室曾报道过从四膜虫匀浆中获得的一种与 NAD 相连的乳酸脱氢酶(LDH)。该部分包含 NADH 和琥珀酸氧化酶系统以及线粒体细胞色素,并进行氧化磷酸化。该制剂催化仅与某些 NAD 类似物结合的 D-和 L-乳酸的氧化;尚未能够证明 NAD 依赖性 D-或 L-乳酸氧化,也没有任何证据表明这些酶中的任何一种是黄素蛋白,这表明它们不能直接还原某些人工电子受体。不存在乳酸外消旋酶。