Isolation of a New Form of Cytochrome P-450 with Prostaglandin A and Fatty Acid w-Hydroxylase Activities from Rabbit Kidney Cortex Microsomes1

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Abstract
Two different forms of cytochrome P-450, highly active in the w-hydroxylation of prosta-glandin A, and the ω- and (ω-l)-hydroxylation of fatty acids (P-450ka-1 and P-450ka-2), have been purified from kidney cortex microsomes of rabbits treated with di(2-ethylhexyl)-phthalate. On the basis of the peptide map patterns and NH2-terminal amino acid sequence, P-450ka-i was determined to be a new form of aω-hydroxylase cytochrome P-460, whereas P-450UB-2 is identical to P-460ka reported earlier. The first 20 NH2-terminal amino acid sequence (ALNPTRLPGSLSGLLQVAGL) and (ALSPTRLPGSFSGFLQAAGL) of P-450ka-1 and P-450Ka-2 showed 90 and 80% homology with that of the lung prostaglandin w-hydroxylase, respectively, suggesting that these three cytochromes P-460 are members of the same w-hydroxylase cytochrome P-460 gene family.