Amino-terminal sequence analysis of six cytochrome P-450 isozymes purified by monoclonal antibody directed immunopurification.
Six hepatic microsomal cytochromes P-450 were isolated from 3-methylcholanthrene induced animals by immunopurification using two monoclonal antibodies. Two forms of cytochromes P-450 (MW 56K and 57K) were from Sprague-Dawley rats, two from C57BL/6 mice (56K and 57K), one form from DBA/2 mice (56K) and one form from guinea pigs (53K). NH2-terminal sequences of the first ten amino acids of these cytochromes P-450 were determined by automated Edman degradation. The 56K polypeptides from rats, C57BL/6 mice, and DBA/2 mice were shown to have identical NH2-terminal sequences. The 57K polypeptides from rats and C57BL/6 mice are homologous to each other but exhibit no homology to 56K polypeptides. The 53K polypeptide from guinea pigs has a unique NH2-terminal sequence with no apparent homology to the other five cytochromes P-450.
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D003577:Cytochrome P-450 Enzyme System / Q000096:biosynthesis / Q000302:isolation & purification*; D004790:Enzyme Induction; D006168:Guinea Pigs; D007527:Isoenzymes / Q000096:biosynthesis / Q000302:isolation & purification*; D008748:Methylcholanthrene / Q000494:pharmacology; D051379:Mice; D008810:Mice, Inbred C57BL; D008811:Mice, Inbred DBA; D008862:Microsomes, Liver / Q000187:drug effects / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D000911:Antibodies, Monoclonal; D007527:Isoenzymes; D008748:Methylcholanthrene; D003577:Cytochrome P-450 Enzyme System