{"title":"Cysteine protease activity in arils of Thaumatococcus daniellii: Relationship between the sweet protein thaumatin and cysteine protease activity","authors":"Andrew G. Stephen , Roy Powls , Robert J. Beynon","doi":"10.1016/0020-711X(94)90080-9","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The intensely sweet protein thaumatin was originally reported to possess autolytic activity, manifest only in the presence of reducing agents. We have shown that the proteolytic activity in partially purified thaumatin preparations is attributable to a cysteine proteinase, thaumatopain, that can be separated from thaumatin by cation exchange chromatography.</p></span></li><li><span>2.</span><span><p>2. Lesser peaks of proteolytic activity coeluted with thaumatin variants, which did not completely exclude the possibility of a weak but inherent proteolytic activity in the thaumatins.</p></span></li><li><span>3.</span><span><p>3. The minor proteolytic peaks were resolved from thaumatins by hydrophobic interaction chromalography, and are probably due to minor charge variants of the thaumatopains. Thaumatin has no intrinsic proteolytic activity.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 7","pages":"Pages 879-884"},"PeriodicalIF":0.0000,"publicationDate":"1994-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90080-9","citationCount":"3","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0020711X94900809","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. The intensely sweet protein thaumatin was originally reported to possess autolytic activity, manifest only in the presence of reducing agents. We have shown that the proteolytic activity in partially purified thaumatin preparations is attributable to a cysteine proteinase, thaumatopain, that can be separated from thaumatin by cation exchange chromatography.
2.
2. Lesser peaks of proteolytic activity coeluted with thaumatin variants, which did not completely exclude the possibility of a weak but inherent proteolytic activity in the thaumatins.
3.
3. The minor proteolytic peaks were resolved from thaumatins by hydrophobic interaction chromalography, and are probably due to minor charge variants of the thaumatopains. Thaumatin has no intrinsic proteolytic activity.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
