Density gradient fractionation of digitonin-treated rat liver plasma membranes and subcellular localization of NADH-oxidoreductase and B-type cytochromes.
Plasma membranes, contaminated very little by endoplasmic reticulum elements, were isolated from rat liver. Activities of NADH-oxidoreductase and b-type cytochromes were higher than expected from this contamination. Between 50 and 80% of these activities were endogenous to plasma membrane. A similar result was obtained after refractionation of digitonin-treated plasma membranes on a sucrose density gradient. This is further evidence for the localization of NADH-ferricyanide reductase, NADH-cytochrome c reductase, and cytochromes b5, P450 and P420 in liver cell membranes.
D000818:Animals; D002458:Cell Fractionation; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D002499:Centrifugation, Density Gradient; D003579:Cytochrome Reductases / Q000302:isolation & purification*; D003573:Cytochrome b Group; D003580:Cytochromes / Q000302:isolation & purification*; D004072:Digitonin / Q000494:pharmacology*; D008099:Liver / Q000201:enzymology* / Q000648:ultrastructure; D008297:Male; D008854:Microscopy, Electron; D009245:NADH Dehydrogenase / Q000302:isolation & purification*; D051381:Rats; D011919:Rats, Inbred Strains; D013347:Subcellular Fractions / Q000201:enzymology
D003573:Cytochrome b Group; D003580:Cytochromes; D003579:Cytochrome Reductases; D009245:NADH Dehydrogenase; D004072:Digitonin