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- W2045708111 abstract "A membrane fraction has been prepared by incubation of microsomes for 10 min at room temperature in a solution which is 0.23% with respect to KCl and 10% with respect to tert.-amyl alcohol. This fraction which sediments as an infranatant layer contains electron-transfer components and activities at a purity about 2-fold greater than in the microsomes. This fraction is enriched in lipid and has the appearance of a vesicular membrane with a uniform repeating subunit structure with a diameter of about 50 Å, similar to that of the original microsome. It is suggested that the microsomal electron-transfer membrane is separable from microsomes because of its greater ability to bind lipid in the presence of tert.-amyl alcohol. A protein complex containing the carbon monoxide-binding pigment (P-450) has been isolated from beef-liver microsomes. The P-450 compound is concentrated 4–5-fold in the isolated complex and the spectrum of the compound is undegraded. The complex contains the following prosthetic groups, flavin, a cytochrome of the b type and non-heme iron. Spectral studies indicate that CO does not react with the cytochrome b, but combines with another component which absorbs strongly at wavelengths shorter than 420 mμ. A protein-lipid complex containing NADH-cytochrome c oxidoreductase activity has been isolated from beef-liver microsomes. The preparation of the enzyme by the successive use of tert.-amyl alcohol, cholate, and ammonium sulfate is described. The enzyme, purified 10- to 15-fold over the microsomes is soluble in the presence of bile acid and contains cytochrome b5 and flavin (FAD) in a 1:1 ratio, phospholipid and non-heme iron." @default.
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- W2045708111 date "1967-01-01" @default.
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- W2045708111 title "The preparation of microsomal electron-transfer complexes" @default.
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- W2045708111 doi "https://doi.org/10.1016/0005-2728(67)90031-x" @default.
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