Specificity of rat liver cathepsin D.

Abstract:

:The specificity of highly purified rat liver cathepsin D was investigated by analyzing the digests of denatured proteins. At the P1 site, cathepsin D prefers hydrophobic residues except Ile and Val, that are branched at the beta-carbon. Strong and weak hydrophobicities are required at P1' and P2 sites, respectively. A lower protency for beta-turn formation is essential for the sequence around the P1 site.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Imoto T,Okazaki K,Koga H,Yamada H

doi

10.1093/jb/101.3.575

subject

Has Abstract

pub_date

1987-03-01 00:00:00

pages

575-80

issue

3

eissn

0021-924X

issn

1756-2651

journal_volume

101

pub_type

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