PURIFICATION OF THE PEROXISOMAL FATTY ACYL-COA OXIDASE FROM RAT-LIVER
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Date
1980
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Abstract
Fatty acyl-CoA oxidase, the rate limiting enzyme of the peroxisomal fatty acid oxidizing system, was purified from rat liver to near homogeneity by a procedure involving affinity chromatography of its apoenzyme on FAD-Sepharose. The oxidase presents an absolute requirement for the dinucleotide which is weakly bound to the apoenzyme (KD, 0.6 .mu.M). The highest specific activity obtained was 27 units/mg protein. The purified enzyme was 2 major polypeptides with apparent MW of 45,000 and 22,000. The enzyme is a flavoprotein with non-covalently bound flavin adenin dinucleotide composed of 4 subunits, 2 of 45,000 MW and 2 of 22,000 MW.