通过一种新型亲和色谱法纯化组织蛋白酶B。
Purification of cathepsin B by a new form of affinity chromatography.
作者信息
Rich D H, Brown M A, Barrett A J
出版信息
Biochem J. 1986 May 1;235(3):731-4. doi: 10.1042/bj2350731.
Abstract
Human cathepsin B was purified by affinity chromatography on the semicarbazone of Gly-Phe-glycinal linked to Sepharose 4B, with elution by 2,2'-dipyridyl disulphide at pH 4.0. The product obtained in high yield by the single step from crude starting material was 80-100% active cathepsin B. The possibility that this new form of affinity chromatography may be of general usefulness in the purification of cysteine proteinases is discussed.
摘要
人组织蛋白酶B通过在与琼脂糖4B偶联的甘氨酰-苯丙氨酰-甘氨醛半卡巴腙上进行亲和层析来纯化，在pH 4.0条件下用2,2'-二吡啶二硫化物洗脱。从粗原料通过单步操作以高产率获得的产物是80 - 100%活性的组织蛋白酶B。讨论了这种新型亲和层析方法在纯化半胱氨酸蛋白酶方面可能具有普遍实用性的可能性。
Zotero 插件