プロスタグランジンω-水酸化活性を有するチトクロームP-450について

概要

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Two forms of cytochrome P-450, designated as cytochrome P-450p-1 and P-450p-2, were separted and purified from lung microsomes of rabbits treated with progesterone. Cytochrome P-450p-1 which catalyze N-demethylation of benzphetamine and O-demethylation of p-nitroanisole, was similar to cytochrome P-450isozyme2 separated from rabbit liver microsomes.On the other hand, cytochrome P-450p-2 catalyze ω-hydroxylation of prostaglandin E_1(PGE_1), prostaglandin E_2(PGE_2), and prostaglandin A_1(PGA_1)as well as ω-and(ω-1)-hydroxylation of palmitate and myristate. This cytochrome showed a greater affinity for prostaglandins than for fatty acids. The amino acid sequence was determined from cloned cDNA of mRNA for cytochromeP-450p-2. The complete polypeptide containe 506 amino acids with a molecular weight of 58,515. The amino acid sequence of cytochrome P-450p-2 showed a low similarity(<25%)to other of cytochrome P-450. These results indicate that cytochrome P-450p-2 is a specific form to play certain role in metabolism of prostaglandins and constitute a unique cytochrome P-450 gene family.
福山大学の論文