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.