Characterization of a new cysteine proteinase inhibitor of human saliva, cystatin SN, which is immunologically related to cystatin S

FEBS Letters

Sanada, Kazuo¹  Saitoh, Eiichi¹  Isemura, Satoko¹ 

[1] Department of Oral Biochemistry, Nippon Dental University, Niigata Faculty, Niigata 951, Japan

关键词: Cysteine proteinase;    Enzyme inhibitor;    Amino acid sequence;    (Human saliva);    Cystatin S;    Cystatin SN;   

DOI  :  10.1016/0014-5793(86)81201-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A new cysteine proteinase inhibitor, cystatin SN, was purified from human whole saliva by chromatography with DE32, Sephacryl S200, and CM-Sepharose CL6B. Cystatin SN is immunologically related to cystatin S and both inhibitors have a similar molecular mass of about 13 kDa. The new inhibitor, however, was clearly distinguished from cystatin S by its much higher pI value. These inhibitors showed similar inhibitory activity for ficin, but cystatin SN was a much better inhibitor for papain and dipeptidyl peptidase I. The amino acid sequence of cystatin SN deduced in the light of the known structure of cystatin S indicates that they have 10 different amino acid residues in the sequence comprising in total 113 residues.

【 授权许可】

Unknown