Organ-specific human alcohol dehydrogenase: isolation and characterization of isozymes from testis |
| |
| Authors: | W P Dafeldecker B L Vallee |
| |
| Affiliation: | 1. Toxicological Center, Department of Pharmaceutical Sciences, Campus Drie Eiken, University of Antwerp, Universiteitsplein 1, 2610 Antwerp, Belgium;2. TICTAC Communications Ltd., St George''s University of London, Cranmer Terrace, London SW170RE, United Kingdom;3. KWR Watercycle Research Institute, Chemical Water Quality and Health, P.O. Box 1072, 3430 BB Nieuwegein, The Netherlands;4. Programme Drugs, Operational Direction of Public health and Surveillance, Scientific Institute for Public Health, Juliette Wytsmanstraat 14, 1050 Brussels, Belgium;5. Institute for Biodiversity and Ecosystem Dynamics, University of Amsterdam, P.O. Box 94248, 1090 GE Amsterdam, The Netherlands |
| |
| Abstract: | Class III alcohol dehydrogenase (ADH) predominates in human testis. The two isozymes of this class were isolated jointly by affinity and conventional ion exchange chromatography. They display anodic electrophoretic mobility at pH 8.2, are completely insensitive to 4-methylpyrazole inhibition and oxidize ethanol and other short-chain primary alcohols very poorly. Thus, their kinetic and inhibition characteristics are identical to human liver class III ADH. In contrast, class I ADH is a barely detectable component of testicular alcohol dehydrogenase. The physicochemical characteristics of class III ADH are virtually identical to those of alcohol dehydrogenases found in other organs. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
