Title : Some properties of a hexadecane hydroxylation system in rabbit intestinal mucosa microsomes.

Pub. Date : 1981 Jun

PMID : 7287656






4 Functional Relationships(s)
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1 Hexadecane hydroxylation activity was solubilized from the intestinal microsomes and reconstituted with a partially purified cytochrome P-450 fraction, and intestinal NADPH-cytochrome c reductase, or spinach ferredoxin and ferredoxin-NADP reductase. n-hexadecane cytochrome P-450 Oryctolagus cuniculus
2 The chromatography of the crude cytochrome P-450 preparation on hydroxylapatite separated at least two cytochrome P-450 fractions; one preferentially hydroxylating hexadecane, and the other preferentially hydroxylating myristic acid. n-hexadecane cytochrome P-450 Oryctolagus cuniculus
3 The chromatography of the crude cytochrome P-450 preparation on hydroxylapatite separated at least two cytochrome P-450 fractions; one preferentially hydroxylating hexadecane, and the other preferentially hydroxylating myristic acid. n-hexadecane cytochrome P-450 Oryctolagus cuniculus
4 The results suggest that rabbit intestinal mucosa microsomes had a cytochrome P-450 species specialized for hexadecane hydroxylation. n-hexadecane cytochrome P-450 Oryctolagus cuniculus