Original scientific paper

Purification of Cathepsin D by Affinity Chromatography on Pepstatin Sepharose Column

I. Kregar ; Department of Biochemistry, J. Stefan Institute, University of Ljubljana, 61000 Ljubljana, Yugoslavia
I. Urh ; Department of Biochemistry, J. Stefan Institute, University of Ljubljana, 61000 Ljubljana, Yugoslavia
H. Umezawa ; Institute of Microbial Chemistry 3-14-23, Kamiosaki, Shinagawa-ku, Tokyo, Japan
V. Turk ; Department of Biochemistry, J. Stefan Institute, University of Ljubljana, 61000 Ljubljana, Yugoslavia

Abstract

A method was developed for the isolation of cathepsin D by
affinity chromatography on immobilized pepstatin. This inhibitor
was coupled to agarose by water soluble carbodiimide. Further
purification included gel filtration on Sephadex G-100. The obtained
cathepsin D exists in three active forms which were resolved on
DEAE cellulose. Electrophoresis in the presence of sodium. dodecyl
sulphate revealed that the first form consists of only one polypeptide
chain having molecular weight 42 000. The second and the third
form contain also polypeptides having molecular weight 27 000
and 14 000.

Keywords

Hrčak ID:

196357

URI

https://hrcak.srce.hr/196357

Publication date:

20.7.1977.

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