Mungikar A M, Gothoskar B P
Res Commun Chem Pathol Pharmacol. 1986 Feb;51(2):281-4.
Cytochrome P-450 was partially purified from human normal granulocytes, using four different purification procedures. PEG-6000 and ammonium sulfate fractionation of human granulocyte post-mitochondrial supernatant (S1) fraction resulted in 3.9 and 2.25 fold purification of cytochrome P-450 respectively. On the other hand, granulocyte S1 fractions subjected to noctylamino sepharose 4B and DEAE cellulose column chromatography separately revealed about 11 fold purification of cytochrome P-450. When these fractions were submitted to SDS-polyacrylamide gel electrophoresis, PEG-6000 and ammonium sulfate precipitated fractions showed multiple protein bands whereas n-octylamino sepharose 4B and DEAE eluates were relatively pure showing one or few bands. There was no indication of the existence of multiple P-450 species in the partially purified human granulocyte cytochrome P-450.
采用四种不同的纯化方法从人正常粒细胞中部分纯化细胞色素P-450。聚乙二醇6000（PEG-6000）和硫酸铵对人粒细胞线粒体后上清液（S1）组分进行分级分离，分别使细胞色素P-450纯化了3.9倍和2.25倍。另一方面，粒细胞S1组分分别经辛基氨基琼脂糖4B和二乙氨基乙基纤维素柱层析，显示细胞色素P-450纯化了约11倍。当这些组分进行十二烷基硫酸钠-聚丙烯酰胺凝胶电泳时，PEG-6000和硫酸铵沉淀的组分显示出多条蛋白带，而正辛基氨基琼脂糖4B和二乙氨基乙基纤维素洗脱液相对较纯，显示出一条或几条带。在部分纯化的人粒细胞细胞色素P-450中没有迹象表明存在多种P-450种类。
