We are analyzing https://link.springer.com/article/10.1007/bf00762467.

Title:
NADH-ascorbate free radical and -ferricyanide reductase activities represent different levels of plasma membrane electron transport | Journal of Bioenergetics and Biomembranes
Description:
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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Topics {✒️}

month download article/chapter nadh-ascorbate free radical clathrin-enriched supernatant added extracellular electron transfer ascorbate free radical plasma membrane represent nadh-ferricyanide reductase activities plasma membrane fractions clathrin-depleted membrane inhibited nadh-afr reductase related subjects electron transport chain privacy choices/manage cookies full article pdf anti-clathrin antiserum nadh ferricyanide reductase august 1993 volume 25 nadh-afr reductase facultad de ciencias nad+ reductase european economic area scope submit manuscript wheat germ agglutinin survive detergent solubilization na+-translocating ferredoxin shewanella oneidensis mr-1 check access instant access conditions privacy policy universidad de córdoba electron transport accepting optional cookies rat liver human cancer prevention journal finder publish plasma membranes ferricyanide reduction article journal article log latest articles https clathrin-depletion article cite biomembranes aims biochemistry 30 enzymology specific activities article villalba privacy policy personal data

Schema {🗺️}

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      headline:NADH-ascorbate free radical and -ferricyanide reductase activities represent different levels of plasma membrane electron transport
      description: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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      dateModified:
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         liver
         ascorbate
         dehydrogenases
         clathrin
         Bioorganic Chemistry
         Biochemistry
         general
         Animal Anatomy / Morphology / Histology
         Animal Biochemistry
         Organic Chemistry
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