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- W1909277103 abstract "Two different forms of cytochrome P-450, highly active in the omega-hydroxylation of prostaglandin A, and the omega- and (omega-1)-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-1 was determined to be a new form of omega-hydroxylase cytochrome P-450, whereas P-450ka-2 is identical to P-450ka 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 omega-hydroxylase, respectively, suggesting that these three cytochromes P-450 are members of the same omega-hydroxylase cytochrome P-450 gene family." @default.
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- W1909277103 date "1989-08-01" @default.
- W1909277103 modified "2023-09-25" @default.
- W1909277103 title "Isolation of a New Form of Cytochrome P-450 with Prostaglandin A and Fatty Acid w-Hydroxylase Activities from Rabbit Kidney Cortex Microsomes1" @default.
- W1909277103 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a122831" @default.
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