ブタ精巣ミクロソームに存在する2種のステロイド-C_<17,20>リアーゼ(Δ^<16>-C_<19>-ステロイド合成酵素及び17α-ヒドロキシラーゼ/リアーゼ)活性の比較

概要

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The comparative study of activities of two enzymes, which were well known as a cleaving enzyme of C_<17>-C_<20> bond of C_<21>-steroids, one was a Δ^<16>-C_<19>-steroid synthetase and the other was a 17α-hydroxylase/lyase, located on testicular microsomes of neonatal pig, were achieved to clarify the property of Δ^<16>-C_<19>-steroid synthetase. Their activities were considerably inhibited by cytochrome P-450-inhibiting compounds such as SU 4885,SU 8000 and SU 10603,but were not inhibited by SKF 525A, o, P'DDD, aminoglutethimide. Furthermore, their activities were remarkably inhibited by CO, various inhibiting agents and temperature of preincubation. Under these experimental conditions, their enzyme activities were inhibited in the same degree. However, on optima for pH and ionic strength, Δ^<16>-C_<19>-steroid synthetase activity was apparently different from 17α-hydroxylase/lyase activity.
公益社団法人日本薬学会の論文
1985-07-25