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- W1496917079 abstract "Abstract An assay of a cyanide-binding protein of rat liver microsomes has been developed based on a cyanide-induced difference spectrum between λmax of 443 nm and λmin of 405 to 410 nm (K = 0.5 mm). The cyanide-binding protein has been isolated by chromatography of deoxycholate-treated microsomes on diethylaminoethylcellulose. Chromatography of a preparation of Nagarse-treated microsomes yielded the cyanide-binding protein free from cytochrome P-450 and cytochrome b5. The absolute spectrum of the purified cyanide-binding protein suggests that the substance is a cytochrome (λmax 410 nm, oxidized; λmax 418, 524, 555 nm, reduced). Preliminary evidence relating the cyanide-binding protein to mixed function oxidation of methyl sterols and stearyl coenzyme A suggests that the protein may function as a component of these oxidases." @default.
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- W1496917079 date "1970-10-01" @default.
- W1496917079 modified "2023-09-28" @default.
- W1496917079 title "Assay and Isolation of a Cyanide-binding Protein of Rat Liver Microsomes" @default.
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- W1496917079 doi "https://doi.org/10.1016/s0021-9258(18)62783-8" @default.
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