NADH-ascorbate free radical and -ferricyanide reductase activities represent different levels of plasma membrane electron transport |
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Authors: | J M Villalba A Canalejo J C Rodríguez-Aguilera M I Burón D James Morré P Navas |
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Institution: | (1) Departamento de Biología Celular, Facultad de Ciencias, Universidad de Córdoba, Córdoba, Spain;(2) Department of Medicinal Chemistry, Purdue University, 47906 West Lafayette, Indiana |
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Abstract: | 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. |
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Keywords: | Plasma membrane liver ascorbate dehydrogenases clathrin |
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