Stimulatory effect of soluble supernatant on hydroxylase activity of rat testis microsomes.
Addition of soluble supernatant to testis microsomes results in 42% increase in steroid 17,20-lyase activity and a 65% increase in 17alpha-hydroxylase activity. This stimulatory activity could be partially purified by salt fractionation. The activating factor(s) was not removed by dialysis nor did it appear to be lipid. It was destroyed by trypsin. Differential effects of heat were observed with the hydroxylase and lyase activators. The activation did not affect Km but only increased Vmax. The supernatant could be added to each enzyme to the point of maturation. No binding of steroids by the supernatant could be detected. Corpus luteum and placental supernatant did not stimulate enzymic activity, but supernatant from an adrenal adenoma was active.
D000818:Animals; D006358:Hot Temperature; D066298:In Vitro Techniques; D008190:Lyases / Q000378:metabolism; D008297:Male; D008861:Microsomes / Q000201:enzymology*; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism; D011374:Progesterone; D051381:Rats; D013254:Steroid 17-alpha-Hydroxylase / Q000378:metabolism; D013347:Subcellular Fractions / Q000378:metabolism / Q000502:physiology*; D013737:Testis / Q000201:enzymology* / Q000502:physiology / Q000648:ultrastructure; D014357:Trypsin / Q000494:pharmacology
D011374:Progesterone; D006899:Mixed Function Oxygenases; D010088:Oxidoreductases; D013254:Steroid 17-alpha-Hydroxylase; D014357:Trypsin; D008190:Lyases