ELECTRON-TRANSFER COMPLEXES OF ASCARIS-SUUM MUSCLE MITOCHONDRIA .1. CHARACTERIZATION OF NADH-CYTOCHROME-C REDUCTASE (COMPLEX I-III), WITH SPECIAL REFERENCE TO CYTOCHROME LOCALIZATION
ELECTRON-TRANSFER COMPLEXES OF ASCARIS-SUUM MUSCLE MITOCHONDRIA .1. CHARACTERIZATION OF NADH-CYTOCHROME-C REDUCTASE (COMPLEX I-III), WITH SPECIAL REFERENCE TO CYTOCHROME LOCALIZATION
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DOI：
10.1016/0166-6851(84)90107-5
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发表时间：
1984-01-01
影响因子：
1.5
通讯作者：
OYA, H
中科院分区：
文献类型：
--
作者：
TAKAMIYA, S;FURUSHIMA, R;OYA, H
从 A. suum 肌肉线粒体中分离出 NADH-细胞色素 c 还原酶（复合体 I-III）。该酶制剂在25℃下催化还原1.68μmol细胞色素c min-1 mg-1蛋白。 C 与 NADH 结合，但不与 NADPH 结合，并且与亚软骨颗粒一样保留其对鱼藤酮、杀粉粉素 A 和 2-庚基-4-羟基喹啉-N-氧化物的敏感性。分离的复合物I-III基本上不含琥珀酸细胞色素c还原酶和细胞色素c氧化酶，由14种多肽组成，表观分子量范围为76,000-12,000。复合物 I-III 含有 3 种细胞色素 6-559.5、6-563 和 c/1-550.5 以及 Pigment-558，浓度分别为 1.28、0.211、1.23 和 0.321 nmol mg-1 蛋白。细胞色素 b-558 是蛔虫线粒体的主要组成细胞色素，之前被认为参与富马酸还原酶系统，但在复合物 I-III 中并未分离。讨论了蛔虫电子转移复合物中细胞色素的定位。
An NADH-cytochrome c reductase (comples I-III) was isolated from A. suum muscle mitochondria. The enzyme preparation catalyzed the reduction of 1.68 .mu.mol cytochrome c min-1 mg-1 protein at 25.degree. C with NADH but not with NADPH, and retained its sensitivity to rotenone, piericidin A and 2-heptyl-4-hydroxyquinoline-N-oxide as with the submitochondrial particles. The isolated complex I-III, essentially free of succinate-cytochrome c reductase and cytochrome c oxidase, consisted of 14 polypeptides with apparent MW ranging from 76,000-12,000. The complex I-III contained 3 cytochromes 6-559.5, 6-563 and c/1-550.5 and Pigment-558 at concentrations of 1.28, 0.211, 1.23 and 0.321 nmol mg-1 protein, respectively. Cytochrome b-558, a major constituent cytochrome of Ascaris mitochondria and previously suggested to participate in the fumarate reductase system, was not fractionated in the complex I-III. Localization of the cytochromes in Ascaris electron transfer complexes is discussed.