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 Biochemjournal_title
Journal of biochemistryauthors
Imoto T,Okazaki K,Koga H,Yamada Hdoi
10.1093/jb/101.3.575subject
Has Abstractpub_date
1987-03-01 00:00:00pages
575-80issue
3eissn
0021-924Xissn
1756-2651journal_volume
101pub_type
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journal_title:Journal of biochemistry
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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journal_title:Journal of biochemistry
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journal_title:Journal of biochemistry
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更新日期:2009-09-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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journal_title:Journal of biochemistry
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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journal_title:Journal of biochemistry
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