{"title":"Agavain: A new plant proteinase","authors":"K.F. Tipton","doi":"10.1016/0926-6569(64)90192-0","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. A procedure is described for the isolation of a crystalline enzyme from crude sisal extract.</p></span></li><li><span>2.</span><span><p>2. The crystalline enzyme has been shown to be homogeneous by electrophoresis, chromatography on DEAE-cellulose, gel filtration on Sephadex, and solubility.</p></span></li><li><span>3.</span><span><p>3. The crystalline enzyme is unstable in solution, changing spontaneously to an inactive protein of smaller molecular weight.</p></span></li><li><span>4.</span><span><p>4. The identity of the crystalline enzyme with Fraction F obtained by chromatography of the crude enzyme of DEAE-cellulose has been demonstrated.</p></span></li><li><span>5.</span><span><p>5. The molecular weight of the enzyme has been determined.</p></span></li><li><span>6.</span><span><p>6. The trivial name agavian has been adopted for the enzyme.</p></span></li></ul></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 2","pages":"Pages 341-350"},"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)90192-0","citationCount":"8","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/0926656964901920","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 8
Abstract
1.
1. A procedure is described for the isolation of a crystalline enzyme from crude sisal extract.
2.
2. The crystalline enzyme has been shown to be homogeneous by electrophoresis, chromatography on DEAE-cellulose, gel filtration on Sephadex, and solubility.
3.
3. The crystalline enzyme is unstable in solution, changing spontaneously to an inactive protein of smaller molecular weight.
4.
4. The identity of the crystalline enzyme with Fraction F obtained by chromatography of the crude enzyme of DEAE-cellulose has been demonstrated.
5.
5. The molecular weight of the enzyme has been determined.
6.
6. The trivial name agavian has been adopted for the enzyme.