Conformation and processing of cathepsin D.

Abstract:

:Cathepsin D occurs in two forms, a single polypeptide chain (Mr 44 000) and a non-covalent complex of two peptides of Mr 14 000 and 30 000 that is derived by proteolytic processing of the 44 000 polypeptide. The two forms from bovine spleen are closely similar in secondary structure content, in aromatic amino acid environment and in the two step denaturation behaviour. Enzyme activity is lost irreversibly on denaturation but conformation can be partially regained. The two separated chains will only refold partially and this is related to their positions in the overall structure of cathepsin D. It is suggested that the processing step is related to protein turnover.

journal_name

Biosci Rep

journal_title

Bioscience reports

authors

Pain RH,Lah T,Turk V

doi

10.1007/BF01119908

subject

Has Abstract

pub_date

1985-10-01 00:00:00

pages

957-67

issue

10-11

eissn

0144-8463

issn

1573-4935

journal_volume

5

pub_type

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