Villalba J M, Canalejo A, Rodríguez-Aguilera J C, Burón M I, Mooré D J, Navas P
Departamento de Biología Celular, Facultad de Ciencias, Universidad de Córdoba, Spain.
J Bioenerg Biomembr. 1993 Aug;25(4):411-7. doi: 10.1007/BF00762467.
Plasma membranes isolated from rat liver by two-phase partition exhibited dehydrogenase activities for ascorbate free radical (AFR) and ferricyanide reduction in a ratio of specific activities of 1:40. NADH-AFR reductase could not be solubilized by detergents from plasma membrane fractions. NADH-AFR reductase was inhibited in both clathrin-depleted membrane and membranes incubated with anti-clathrin antiserum. This activity was reconstituted in plasma membranes in proportion to the amount of clathrin-enriched supernatant added. NADH ferricyanide reductase was unaffected by both clathrin-depletion and antibody incubation and was fully solubilized by detergents. Also, wheat germ agglutinin only inhibited NADH-AFR reductase. The findings suggest that NADH-AFR reductase and NADH-ferricyanide reductase activities of plasma membrane represent different levels of the electron transport chain. The inability of the NADH-AFR reductase to survive detergent solubilization might indicate the involvement of more than one protein in the electron transport from NADH to the AFR but not to ferricyanide.
通过两相分配从大鼠肝脏分离的质膜对抗坏血酸自由基（AFR）表现出脱氢酶活性，对铁氰化物还原的比活性为1:40。NADH-AFR还原酶不能被去污剂从质膜组分中溶解。NADH-AFR还原酶在网格蛋白缺失的膜和与抗网格蛋白抗血清孵育的膜中均受到抑制。该活性在质膜中与添加的富含网格蛋白的上清液量成比例地重建。NADH铁氰化物还原酶不受网格蛋白缺失和抗体孵育的影响，并且完全可被去污剂溶解。此外，麦胚凝集素仅抑制NADH-AFR还原酶。这些发现表明质膜的NADH-AFR还原酶和NADH-铁氰化物还原酶活性代表电子传递链的不同水平。NADH-AFR还原酶不能在去污剂溶解后存活可能表明从NADH到AFR但不是到铁氰化物的电子传递涉及不止一种蛋白质。
