A dehydroepiandrosterone sulfatase inhibitory activity in soluble proteins of guinea pig liver |
| |
| Authors: | M Moutaouakkil G L Adessi |
| |
| Affiliation: | 1. Division of Molecular and Systems Toxicology, Department of Pharmaceutical Sciences, University of Basel, Basel, Switzerland;2. Swiss Centre for Applied Human Toxicology, Department of Pharmaceutical Sciences, University of Basel, Basel, Switzerland;1. Genitourinary Malignancies Research Center, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, United States;2. Department of Urology, Glickman Urological and Kidney Institute, Cleveland Clinic, Cleveland, OH, United States;3. Department of Hematology and Oncology, Taussig Cancer Institute, Cleveland Clinic, Cleveland, OH, United States |
| |
| Abstract: | 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. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
