Kee Min Woo , Woelsung Yi , Young Jong Sohn , Chung-Soon Chang , Man-Sik Kang , Doo Bong Ha , Chin Ha Chung
{"title":"Purification and characterization of a poly-l-lysine-activated serine endoprotease from Lumbricus rubellus","authors":"Kee Min Woo , Woelsung Yi , Young Jong Sohn , Chung-Soon Chang , Man-Sik Kang , Doo Bong Ha , Chin Ha Chung","doi":"10.1016/0305-0491(94)90143-0","DOIUrl":null,"url":null,"abstract":"<div><p>An endoprotease in earthworm (<em>Lumbricus rubellus</em>) is purified to apparent homogeneity using <sup>125</sup>I-lactalbumin as a substrate. The protease has a molecular mass of 27 kDa and is markedly activated by poly-<span>l</span>-lysine or poly-<span>l</span>-arginine. It is a chymotrypsin-like serine protease. Its activity is distributed to coelomic fluid but relatively little to coelomocytes.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 1","pages":"Pages 71-80"},"PeriodicalIF":0.0000,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90143-0","citationCount":"7","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0305049194901430","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 7
Abstract
An endoprotease in earthworm (Lumbricus rubellus) is purified to apparent homogeneity using 125I-lactalbumin as a substrate. The protease has a molecular mass of 27 kDa and is markedly activated by poly-l-lysine or poly-l-arginine. It is a chymotrypsin-like serine protease. Its activity is distributed to coelomic fluid but relatively little to coelomocytes.