{"title":"部分降解唾液胱抑素的抑制活性","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":"{\"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}","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}
Inhibitory activities of partially degraded salivary cystatins
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.
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