{"title":"Fractionation of proteolytic enzymes from sisal (Agave sisalanus) on deae-cellulose","authors":"K.F. Tipton","doi":"10.1016/0926-6569(64)90191-9","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Crude sisal extract has been fractionated into seven protein components by chromatography on DEAE-cellulose.</p></span></li><li><span>2.</span><span><p>2. Each component was shown to be essentially homogeneous on rechromatography on DEAE-cellulose and on gel filtration on Sephadex G 100.</p></span></li><li><span>3.</span><span><p>3. Five of the components were shown to have proteolytic activity toward casein and four had amidase activity toward α-benzoyl-<span>l</span>-arginine amide.</p></span></li><li><span>4.</span><span><p>4. Four of the active components were found to be inhibited by metal binding agents and di-isopropylphosphorofluoridate.</p></span></li><li><span>5.</span><span><p>5. None of the active components appeared to depend on a sulphydryl group for activity.</p></span></li><li><span>6.</span><span><p>6. The components differed in their specific activities, pH optima, and molelcular weights as indicated by gel filtration on Sephadex G 100.</p></span></li></ul></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 2","pages":"Pages 334-340"},"PeriodicalIF":0.0000,"publicationDate":"1964-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90191-9","citationCount":"5","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926656964901919","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 5
Abstract
1.
1. Crude sisal extract has been fractionated into seven protein components by chromatography on DEAE-cellulose.
2.
2. Each component was shown to be essentially homogeneous on rechromatography on DEAE-cellulose and on gel filtration on Sephadex G 100.
3.
3. Five of the components were shown to have proteolytic activity toward casein and four had amidase activity toward α-benzoyl-l-arginine amide.
4.
4. Four of the active components were found to be inhibited by metal binding agents and di-isopropylphosphorofluoridate.
5.
5. None of the active components appeared to depend on a sulphydryl group for activity.
6.
6. The components differed in their specific activities, pH optima, and molelcular weights as indicated by gel filtration on Sephadex G 100.