DOI: 10.1042/bj2350731. Purification of cathepsin B by a new form of affinity chromatography

Purification of cathepsin B by a new form of affinity chromatography

10.1042/bj2350731

Crossref journal-article

Portland Press Ltd.

Biochemical Journal (288)

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.

Bibliography

Rich, D. H., Brown, M. A., & Barrett, A. J. (1986). Purification of cathepsin B by a new form of affinity chromatography. Biochemical Journal, 235(3), 731â734.

Authors 3

D H Rich (first)
M A Brown (additional)
A J Barrett (additional)

References 0 Referenced 53

None

Dates

Type	When
Created	10 years ago (Aug. 10, 2015, 4:53 p.m.)
Deposited	3 years, 9 months ago (Nov. 25, 2021, 11 a.m.)
Indexed	1 year, 9 months ago (Oct. 31, 2023, 5:05 a.m.)
Issued	39 years, 3 months ago (May 1, 1986)
Published	39 years, 3 months ago (May 1, 1986)
Published Print	39 years, 3 months ago (May 1, 1986)

Funders 0

None

BibTeX

@article{Rich_1986, title={Purification of cathepsin B by a new form of affinity chromatography}, volume={235}, ISSN={1470-8728}, url={http://dx.doi.org/10.1042/bj2350731}, DOI={10.1042/bj2350731}, number={3}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Rich, D H and Brown, M A and Barrett, A J}, year={1986}, month=may, pages={731–734} }

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