| 应用 |
A protease that cleaves proteins on the carboxyl bond of arginine |
| 产品介绍 |
Clostripain (Endoproteinase-Arg-C) is a two chain proteinase associated with collagenase and isolated from Clostridium histolyticum. It is highly specific for the carboxyl peptide bond of arginine. Clostripain has a sulfhydryl requirement; it is activated by dithiothreitol, cysteine, or other sulfhydryl containing reagents. The presence of calcium ions is essential. The enzyme is inhibited by oxidizing agents and sulfhydryl reactants and by Co2+, Cu2+, Cd2+, and heavy metal ions. Citrate, borate, and Tris anions are less inhibitory. |
| 备注 |
Chromatographically purified. A dialyzed, lyophilized pre-activated powder. |
| 生化机理 |
Clostripain from Clostridium histolyticum is composed of two polypeptide chains, with molecular masses of 41.7 kDa and 15.4 kDa. Clostripain has a highly restricted substrate specificity for Arg-Xaa peptide bonds. Therefore, clostripain has been explored as a potential enzyme for protein sequencing purposes. It has also been studied as a catalyst for condensation of pharmaceutically important peptides containing Arg-Pro bonds. |
| 别名 |
;Endoproteinase-Arg-C;Clostridiopeptidase B;Proteinase from Clostridium histolyticum |
