Proteolytically active complexes of cathepsin L and a cysteine proteinase inhibitor; purification and demonstration of their formation in vitro.
Proteolytically active complexes of cathepsin L and a cysteine proteinase inhibitor; purification and demonstration of their formation in vitro.
复制标题
组织蛋白酶 L 和半胱氨酸蛋白酶抑制剂的蛋白水解活性复合物；
DOI：
10.1016/0003-9861(92)90734-e
复制
发表时间：
1992
影响因子：
3.9
通讯作者：
C. Dennison
中科院分区：
文献类型：
--
作者：
R. Pike;T. Coetzer;C. Dennison
从羊肝脏中纯化出具有半胱氨酸蛋白酶内源性抑制剂的蛋白酶组织蛋白酶L的蛋白水解活性复合物。该配合物对合成底物z - phesing单键、单键、hmec、偶氮酪蛋白和明胶均有活性。经过还原和非还原十二烷基硫酸钠-聚丙烯酰胺凝胶电泳，用纯化的羊肝组织蛋白酶L和纯化的羊肝半胱氨酸蛋白酶抑制剂（可能是stefin B）的单特异性抗体培养，Western blotting证实了复合物的组成。在体外，纯化的羊肝组织蛋白酶L与纯化的羊肝胱抑素在pH为5.5或更高的条件下共孵育，也可以形成类似的复合物。
Proteolytically active complexes of the proteinase cathepsin L, with an endogenous inhibitor of cysteine proteinases, were purified from sheep liver. The complexes were active against the synthetic substrate Z-Phesingle bondArgsingle bondNHMec and also the proteins azocasein and gelatin. The composition of the complexes was demonstrated by Western blotting, after reducing and nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis with monospecific antibodies raised against purified sheep liver cathepsin L and purified sheep liver cysteine proteinase inhibitor (probably stefin B). Similar complexes could be formedin vitro, by coincubation of purified sheep liver cathepsin L with the purified sheep liver cystatin at a pH of 5.5 or higher.
膜相关组织蛋白酶 L：在黑色素瘤转移中的作用。
DOI：
10.1016/0006-291x(89)91755-5
发表时间：
1989
影响因子：
3.1
作者：
Rozhin,J;Wade,RL;Honn,KV;Sloane,BF
通讯作者：
Sloane,BF