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. 1986 May 1;235(3):731-4.
doi: 10.1042/bj2350731.

Purification of cathepsin B by a new form of affinity chromatography

D H Rich, M A Brown, A J Barrett

Purification of cathepsin B by a new form of affinity chromatography

D H Rich et al. Biochem J. .

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.

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