作　　者： ; ; ; ; ;

机构地区： 首都医学院

出　　处： 《首都医学院学报》 1992年第1期10-14,共5页

摘　　要： 改进了从猪胰中提取羧肽酶B的方法,使回收率提高到15％,比活性增加到192U/mg蛋白,酶的纯度达到91％。 For enhancing the purification recovery of carboxypeptidase B, the Felk' s method was modified as following: (1)Both of Tris-HCl buffers with contained 0. 1 mol/L and 0. 15 mol/L NaCl were ap- plied respectively in the batch adsorption and elution from DEAE-cellulose. (2)In the second DEAE-cellulose chromatography, the DEAE-cellulose column was e- luted with linear gradient of NaCl from 0.00 to 0.09 mol/L in Tris-HAc buffer. (3)Carboxypeptidase B was eluted completely with 0. 09 mol/L NaCl in Tris-HAc buffer. The purity and the molecular weight were identified by TLC scanning method after gel electrophoresis. The results showed that recovery of enzyme activity was in creased from 8% to 15%, specific activity was increased from 175 U/mg to 192 U/mg and purity of en- zyme was reached 91%.

关 键 词： 羧基肽酶 猪胰 分离 纯化

领　　域： [化学工程]