Purification of cathepsin B by a new form of affinity chromatography
- 1 May 1986
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 235 (3) , 731-734
- https://doi.org/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.This publication has 16 references indexed in Scilit:
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