Ichihara K, Kasaoka I, Kusunose E, Kusunose M
J Biochem. 1980 Feb;87(2):671-4. doi: 10.1093/oxfordjournals.jbchem.a132793.
Benzo(a)pyene hydroxylation activity was solubilized from rabbit intestinal mucosa microsomes and reconstituted with a cytochrome P-450 preparation obtained by fractionation with 6-amino-n-hexyl Sepharose 4B, hydroxylapatite and CM-Sephadex C-50, and partially purified NADPH-cytochrome c reductase. Phosphatidylserine was required for the maximal activity, while phosphatidylcholine had no stimulatory effect. The carbon monoxide difference spectrum of the cytochrome P-450 fraction showed a maximum peak at 450 nm. Although another cytochrome P-450 fraction was active for hexadecane hydroxylation, this fraction had little activity. The results indicate that more than one cytochrome P-450 exists in the intestinal mucosa microsomes.
苯并(a)芘羟化活性从兔小肠黏膜微粒体中溶解出来，并与通过用6-氨基正己基琼脂糖4B、羟基磷灰石和CM-葡聚糖凝胶C-50分级分离获得的细胞色素P-450制剂以及部分纯化的NADPH-细胞色素c还原酶一起重构。最大活性需要磷脂酰丝氨酸，而磷脂酰胆碱没有刺激作用。细胞色素P-450组分的一氧化碳差光谱在450nm处有一个最大峰。虽然另一个细胞色素P-450组分对十六烷羟化有活性，但该组分活性很小。结果表明，小肠黏膜微粒体中存在不止一种细胞色素P-450。
