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- W1999532023 abstract "The cytochrome P-450 of gonadal microsomes is an integral component of the steroid converting enzymes, 17α-hydroxylase and 17,20-lyase. Interaction of the steroid substrates with this cytochrome results in a shift in the Soret band as measured by difference spectroscopy. In these studies it is shown that in contrast to placental microsomal cytochrome P-450 which binds C19, steroids, testis microsomal cytochrome P-450 primarily binds C, steroids. However, addition of a 17α-methyl, 17β-acetate or a 17β-benzoate group to testosterone permits interaction. The addition of hydroxyl or methyl groups to other positions does not affect binding. The presence of multiple oxygen functions on C21 steroids, as in cortisol and corticosterone, precludes interaction. At least one oxygen function seems necessary for binding as 5α- and 5β-pregnane do not bind whereas 20-deoxypregnenolone (5-pregnen-3β-ol) does bind. These findings indicate that factors in addition to hydrophobic interactions dictate the binding of steroid substrates to testis microsomal cytochrome P-450." @default.
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- W1999532023 date "1956-10-01" @default.
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- W1999532023 title "The biosynthesis of radioactive 17β-estradiol. II. Synthesis by testicular and ovarian homogenates" @default.
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- W1999532023 doi "https://doi.org/10.1016/0003-9861(56)90271-5" @default.
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