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- W2052944321 abstract "Aromatase cytochrome P-450 has been purified from human placenta to homogeneity, as demonstrated by electrophoresis on polyacrylamide gels with SDS, and by double diffusion against an antibody raised in rabbits. The enzyme converts androstenedione to estrone (Vmax 13.3 n moles/min/n mole P-450; Km 30 μM) and testosterone to estradiol. Aromatase activity requires P-450, P-450 reductase and NADPH. Enzyme activity is inhibited by anti-aromatase antibodies and by 4-hydroxyandrostenedione. The enzyme shows a molecular weight of 55,000, is extremely unstable and spontaneously forms P-420 with a half-life of 2.5 days." @default.
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- W2052944321 date "1986-01-01" @default.
- W2052944321 modified "2023-09-27" @default.
- W2052944321 title "Purification to homogeneity of aromatase from human placenta" @default.
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- W2052944321 doi "https://doi.org/10.1016/s0006-291x(86)80477-6" @default.
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