Partial purification of cytochrome P-450 from human normal granulocytes.
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.
D000645:Ammonium Sulfate; D002847:Chromatography, Agarose; D002848:Chromatography, DEAE-Cellulose; D003577:Cytochrome P-450 Enzyme System / Q000097:blood* / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D006098:Granulocytes / Q000032:analysis*; D006801:Humans; D011092:Polyethylene Glycols
D011092:Polyethylene Glycols; D003577:Cytochrome P-450 Enzyme System; D000645:Ammonium Sulfate