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- W1993951917 abstract "A cytochrome P-450 (P-450), designated P-450HKω, has been isolated and purified from human kidney microsomes to a specific content of 13 nmoles of P-450/mg of protein. P-450HKω showed an apparent molecular weight of 52,000 on sodium dodecyl sulfate-polyaerylamide gel electrophoresis (SDS-PAGE). Absolute spectra of the oxidized form indicated that this P-450 was largely in the low-spin state and partly in the high-spin state. It catalyzed the ω-and (ω − 1)-hydroxylation of fatty acids such as laurate, myristate, and palmitate, with no activity toward prostaglandin A1, benzphetamine, 7-ethoxycoumarin, or 7-ethoxyresorufin. The first 35 NH2-terminal amino acid sequence of P-450HKω had about 70% homology with those of rabbit kidney fatty acid ω-hydroxylases of the P-450 IVA gene subfamily, P-450ka-1, P-450ka-2, and P-450kd, except for four undetermined residues. Moreover, Western blot and immuno-inhibition studies showed that P-450HKω reacted with an antibody against the rabbit kidney fatty acid ω-hydroxylase. The results suggest that P-450HKω is a member of the same P-450 gene family (IVA subfamily) as the rabbit enzymes. In addition, the terminal sequence of P-450HKω also showed 54% homology with that of P-450k-2, a fatty acid ω-hydroxylase from rat kidney microsomes. To our knowledge, this is the first time that a P-450 specific for fatty acid ω-hydroxylase activity has been isolated to homogeneity from human tissues." @default.
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- W1993951917 date "1992-01-01" @default.
- W1993951917 modified "2023-09-27" @default.
- W1993951917 title "Purification and NH2-terminal amino acid sequences of human and rat kidney fatty acid ω-hydroxylases" @default.
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- W1993951917 doi "https://doi.org/10.1016/0005-2760(92)90106-6" @default.
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