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- W1964046210 abstract "Fatty acyl-CoA oxidase, the rate limiting enzyme of the peroxisomal fatty acid oxidizing system, has been purified from rat liver to near homogeneity by a procedure involving affinity chromatography of its apoenzyme on flavin adenin dinucleotide-Sepharose. The oxidase presents an absolute requirement for the dinucleotide which is weakly bound to the apoenzyme (KD, 0.6 μM). The highest specific activity obtained was 27 units/mg protein. The purified enzyme has two major polypeptides with apparent molecular weights of 45,000 and 22,000. These results suggest that the enzyme is a flavoprotein with non covalently bound flavin adenin dinucleotide composed of four subunits, two of 45,000 m.w. and two of 22,000 m.w." @default.
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- W1964046210 date "1980-07-01" @default.
- W1964046210 modified "2023-09-25" @default.
- W1964046210 title "Purification of the peroxisomal fatty acyl-CoA oxidase from rat liver" @default.
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- W1964046210 doi "https://doi.org/10.1016/0006-291x(80)90696-8" @default.
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