A dehydroepiandrosterone sulfatase inhibitory activity in soluble proteins of guinea pig liver.
An inhibitor of microsomal dehydroepiandrosterone sulfatase was found in the soluble fraction of non-pregnant guinea pig liver. The extent of inhibitory effect was dependent on the concentration of soluble proteins. The inhibitor was partly purified by gel permeation and hydroxylapatite chromatography with a purification factor of 16.6. The soluble inhibitor was non-dialyzable, not destroyed by RNase or DNase digestion but totally destroyed by pronase digestion. The inhibitor is a soluble protein with a molecular weight of approximately 17,000 (determined by gel permeation chromatography). Inhibition of microsomal dehydroepiandrosterone sulfatase by the soluble inhibitor is a non-competitive inhibition. From this present finding the question arises whether the inhibitor could be involved in the regulation of the hydrolysis of dehydroepiandrosterone sulfate in the guinea pig liver.
D000818:Animals; D002850:Chromatography, Gel; D017886:Durapatite; D005260:Female; D006168:Guinea Pigs; D006882:Hydroxyapatites; D007700:Kinetics; D008099:Liver / Q000032:analysis*; D008970:Molecular Weight; D011247:Pregnancy; D011402:Pronase; D011506:Proteins / Q000302:isolation & purification; D043266:Steryl-Sulfatase; D013429:Sulfatases / Q000037:antagonists & inhibitors*
D006882:Hydroxyapatites; D011506:Proteins; D017886:Durapatite; D013429:Sulfatases; C020121:estrone sulfatase; D043266:Steryl-Sulfatase; D011402:Pronase