ブタ副腎ミクロソームのステロイド17α-ヒドロキシラーゼ-C<SUB>17,20</SUB>リアーゼ(チトクロームP-450) : プロゲステロンによるリアーゼ活性の阻害と17α-ヒドロキシプロゲステロンによるヒドロキシラーゼ活性の阻害

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タイトル別名
  • Steroid 17α-Hydroxylase-C<SUB>17, 20</SUB> lyase (Cytochrome P-450) from Porcine Adrenocortical Microsomes : Inhibition of Lyase Activity by Progesterone, and Inhibition of Hydroxylase Activity by 17α-Hydroxyprogesterone
  • ブタ副腎ミクロソームのステロイド17α-ヒドロキシラーゼーC17,20リアーゼ(チトクロームP-450)--プロゲステロンによるリアーゼ活性の阻害と17α-ヒドロキシプロゲステロンによるヒドロキシラーゼ活性の阻害
  • ブタ フクジン ミクロソーム ノ ステロイド 17 アルファ ヒドロキシラーゼ
  • Steroid 17&alpha;-Hydroxylase-C<SUB>17, 20</SUB> lyase (Cytochrome P-450) from Porcine Adrenocortical Microsomes : Inhibition of Lyase Activity by Progesterone, and Inhibition of Hydroxylase Activity by 17&alpha;-Hydroxyprogesterone

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説明

Highly purified 17α-hydroxylase-C17, 20 lyase (cytochrome P-450) from porcine adrenocortical microsomes was incubated with [4-14C]-C21-steroid substrate in the presence of cytochrome P-450 reductase and nicotinamide adenine dinucleotide phosphate as a cofactor. On the kinetic analysis, C17, 20 lyase activity was strongly inhibited by progesterone. The inhibition was competitive, and K1 value for progesterone was 0.9μM. In addition, 17α-hydroxylase activity was inhibited by 17α-hydroxyprogesterone. The inhibition was competitive, and K1 value for 17α-hydroxyprogesterone was 7.5μM. These results suggest that both hydroxylase and lyase reactions are catalyzed on a single active site.

収録刊行物

  • 薬学雑誌

    薬学雑誌 105 (1), 83-85, 1985

    公益社団法人 日本薬学会

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