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Endocrinology, Vol 107, 1055-1060, Copyright © 1980 by Endocrine Society

ARTICLES

Reconstitution of steroid 17,20-lyase activity after separation and purification of cytochrome P-450 and its reductase from rat testis microsomes

G Betz, P Tsai and D Hales

The testicular enzyme, 17,20-lyase, catalyzes the removal of the C-17 side chain from steroids in the synthesis of androgens. This activity employs cytochrome P-450 as an oxygen donor. Attempts to purify the cytochrome and its reductase from testis microsomes have previously been unsuccessful due to the low concentrations of these components (2-- 5% that of liver). The cytochrome and reductase were solubilized from rat testis microsomes using a mixture of sodium cholate and Emulgen 913. The components were then separated by DEAE chromatography. The cytochrome was further purified by chromatography using hydroxylapatite for an 8.5-fold enrichment. The reductase was further purified by hydroxylapatite and affinity chromatography. An 84-fold enrichment was achieved. 17,20-Lyase activity could be partially restored by mixing the cytochrome and reductase in the presence of phospholipid.




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Copyright © 1980 by The Endocrine Society