[Latent form of glutathione reductase in the rat liver].
The existence of membrane-bound forms of glutathione reductase in rat liver and transplantable hepatoma G-27 was demonstrated, using differential centrifugation techniques. The activity of the sedimentable form of the liver enzyme was detected only in the presence of detergents. Conditions for the manifestation of the latent glutathione reductase activity in whole liver homogenates and in the 105000 g pellet were determined. Solubilization of the latent form of the enzyme in the presence of sodium deoxycholate increases 2-fold the glutathione reductase activity in liver homogenates (but not in hepatoma). Simultaneous determination of the disulfidereductase, nonspecific NADPH-oxidase and gamma-glutamyltransferase (membrane-bound enzyme of glutathione metabolism) activities was performed.
Chernov
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D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D003840:Deoxycholic Acid / Q000494:pharmacology; D003902:Detergents / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D005980:Glutathione Reductase / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008114:Liver Neoplasms, Experimental / Q000201:enzymology*; D008297:Male; D009252:NADPH Dehydrogenase / Q000378:metabolism; D051381:Rats; D012995:Solubility; D013880:Thioredoxin-Disulfide Reductase / Q000378:metabolism; D005723:gamma-Glutamyltransferase / Q000378:metabolism
D003902:Detergents; D003840:Deoxycholic Acid; D009252:NADPH Dehydrogenase; D005980:Glutathione Reductase; D013880:Thioredoxin-Disulfide Reductase; D005723:gamma-Glutamyltransferase
Latentnaia forma glutationreduktazy v pecheni krys.