从猪胰脏粉末中亲和纯化激肽释放酶和弹性蛋白酶。
Affinity purification of kallikrein and elastase from hog pancrease powder.
作者信息
Honda T, Fujita A, Tsubakihara Y, Morihara K
出版信息
J Chromatogr. 1986 Apr 11;376:385-93. doi: 10.1016/s0378-4347(00)80854-3.
The present report describes a method that is efficient for simultaneous isolation of kallikrein and elastase from hog pancrease powder. Both enzymes were separated by successive column chromatography on CM-cellulofine and p-aminobenzamidine-Sepharose 4B. Kallikrein was further purified by column chromatography on DEAE-Sephadex and elastase was purified by repeated gel chromatography on Sephadex G-75. The kallikrein obtained was composed of two components, which were separable by sodium dodecyl sulphate polyacrylamide gel electrophoresis, and the elastase had one component. The activity yields of kallikrein and elastase were 49 and 38%, respectively.
本报告描述了一种从猪胰脏粉末中同时高效分离激肽释放酶和弹性蛋白酶的方法。两种酶通过在CM-纤维素和对氨基苯甲脒-琼脂糖4B上连续进行柱色谱分离。激肽释放酶通过在DEAE-葡聚糖凝胶上进行柱色谱进一步纯化，弹性蛋白酶通过在葡聚糖凝胶G-75上反复进行凝胶色谱纯化。所获得的激肽释放酶由两个组分组成，这两个组分可通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳分离，而弹性蛋白酶只有一个组分。激肽释放酶和弹性蛋白酶的活性产率分别为49%和38%。
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