Isolation of Cathepsin D by Affinty Chromatography on Immobilized Pepstatin View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1977

AUTHORS

I. Kregar , I. Urh , R. Smith , H. Umezawa , V. Turk

ABSTRACT

Affinity chromatography with an immobilized substrate proved to be a successful tool in the preparation of pure and undegraded cathepsin D (1). Immobilized reversible inhibitors are even more suitable for the isolation because the enzyme remains inactive during the affinity chromatography procedure. Pepstatin is known as a strong inhibitor of carboxyl proteases (2) and we wanted to make use of its inhibitory property for the isolation of cathepsin D. In this report, a method for isolation of cathepsin D is described using affinity chromatography on pepstatin-agarose. More... »

PAGES

250-254

Book

TITLE

Intracellular Protein Catabolism II

ISBN

978-1-4615-8815-3
978-1-4615-8813-9

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4615-8813-9_31

DOI

http://dx.doi.org/10.1007/978-1-4615-8813-9_31

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042260786


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