Patil S S, Makhija S J, Pawar S S
Chemistry Department, S.B.E.S. Science College, Aurangabad.
Indian J Biochem Biophys. 1992 Dec;29(6):516-8.
Cytochrome P-450 has been purified from goat and chick erythrocytes and characterized. Goat erythrocyte cytochrome P-450 content was higher than that of chick erythrocytes cytochrome P-450. Elution profile of purified protein from DEAE-cellulose column showed a single peak. The catalytic activities of aminopyrine-N-demethylase and acetanilide hydroxylase were found to be higher in purified proteins. Molecular weight was determined by SDS-polyacrylamide gel electrophoresis.
细胞色素P-450已从山羊和鸡的红细胞中纯化并进行了特性鉴定。山羊红细胞细胞色素P-450的含量高于鸡红细胞细胞色素P-450。从DEAE-纤维素柱上洗脱纯化蛋白的图谱显示为单峰。在纯化蛋白中发现氨基比林-N-脱甲基酶和乙酰苯胺羟化酶的催化活性较高。通过SDS-聚丙烯酰胺凝胶电泳测定分子量。
