作者: PIERRE CHAPDELAINE , JEAN Y. DUBÉ , GILLES FRENETTE , ROLAND R. TREMBLAY
DOI: 10.1002/J.1939-4640.1984.TB02395.X
关键词: Isoelectric point 、 Serine protease 、 Polyacrylamide gel electrophoresis 、 Proteases 、 Biology 、 Chromatofocusing 、 Serine 、 Molecular mass 、 Molecular biology 、 Sephadex 、 Biochemistry
摘要: This work was undertaken to determine the identity of major androgen-dependent 15,000 molecular weight protein previously observed on SDS polyacrylamide gel electrophoresis both dog prostate cytosol and seminal plasma. The identified as one two chains arginine esterase basis its ability bind 3H-diisopropylphosphofluoridate (DFP), an active site titrant serine proteases. Furthermore, since other polypeptide chain heterogeneous, at least five distinct peaks activity could be separated by chromatofocusing under nonreducing conditions. plasma estimated 29,500 Sephadex G-100 filtration, 25,000 in absence mercaptoethanol. In presence mercaptoethanol, were with weights 14,000. These results show that is a protease composed different linked disulfide bridges. One contains reactive group. probably glycosylated it presents several isoelectric points.