{"title":"Inhibitory activities of partially degraded salivary cystatins","authors":"Satoko Isemura , Eiichi Saitoh","doi":"10.1016/0020-711X(94)90112-0","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Aminoterminally truncated forms of cystatin S and cystatin SN had higher inhibition constants for ficin, but lower ones for cathepsin C (dipeptidyl peptidase I) as compared to their respective full-sized form.</p></span></li><li><span>2.</span><span><p>2. Cystatin SN still retained the inhibitory activity for ficin after reduction and carboxymethylation, although the inhibition constant increased.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 6","pages":"Pages 825-831"},"PeriodicalIF":0.0000,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90112-0","citationCount":"3","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0020711X94901120","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 3
Abstract
1.
1. Aminoterminally truncated forms of cystatin S and cystatin SN had higher inhibition constants for ficin, but lower ones for cathepsin C (dipeptidyl peptidase I) as compared to their respective full-sized form.
2.
2. Cystatin SN still retained the inhibitory activity for ficin after reduction and carboxymethylation, although the inhibition constant increased.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
