Abstract:
:A cysteine proteinase inhibitor (designated as cystatin SA) was isolated from human whole saliva by procedures including chromatography on DE 32 and DEAE-Sepharose CL-6B. The amino acid sequence determined by conventional methods showed sequence homology of 90 and 87% as compared with the sequences of cystatin S and cystatin SN, respectively, both of which are salivary inhibitors characterized previously. The new inhibitor consisted of 117 residues and had a pI value of 4.3. Cystatin SA inhibited ficin and papain more strongly than cystatin S or cystatin SN did. It also exhibited inhibitory activity toward dipeptidyl peptidase I but the activity was much weaker than those toward ficin and papain.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Isemura S,Saitoh E,Sanada Kdoi
10.1093/oxfordjournals.jbchem.a122107subject
Has Abstractpub_date
1987-10-01 00:00:00pages
693-704issue
4eissn
0021-924Xissn
1756-2651journal_volume
102pub_type
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