{SNA} 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Clostripain, Enzyme Class Index, Enzymes, Inhibitors, and Substrates, Proteases, Proteases & Protein Sequencing, Proteolytic Enzymes, Proteolytic Enzymes and Substrates, Selective Proteolyt
{SNA} 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Clostripain, Enzyme Class Index, Proteases, Proteases & Protein Sequencing, Proteolytic Enzymes, Proteolytic Enzymes and Substrates, Selective Proteolytic Enzymes, 酶、抑制剂和底物
{SNA} 3.4.x.x Peptidases,
产品应用
A protease that cleaves proteins on the carboxyl bond of arginine
相关文献及参考
Olge Jdand Tytell AA., The activity of Clostridium histolyticum proteinase on synthetic substrates. Arch. Biochem. Biophys. 42(2) , 327-36, (1953)
Nishimura J.S., et al, Sensitivity of Escherichia coli succinyl-CoA mutants at Trp β 76 to clostripain and to trypsin. ADP and ATP protect against cleavage by clostripain at Arg β 80. J. Biol. Chem. 268(18) , 13717-22, (1993)
Guzik K., et al, A new insight into phagocytosis of apoptotic cells: proteolytic enzymes divert the recognition and clearance of polymorphonuclear leukocytes by macrophages Cell Death Differ. 14 , 171-182, (2007) 摘要
安全信息
WGK Germany
3
Personal Protective Equipment
Eyeshields, Gloves, type N95 (US), type P1 (EN143) respirator filter
Storage condition
储存温度2-8℃
其他信息
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.