{"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.

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又是一种新的植物蛋白酶
1.1. 描述了从粗剑麻提取物中分离结晶酶的方法。2.2。通过电泳、deae -纤维素层析、Sephadex凝胶过滤和溶解度证明该结晶酶是均匀的。结晶酶在溶液中是不稳定的,会自发地变成一种分子量较小的无活性蛋白质。通过deae纤维素粗酶层析得到的结晶酶与F组分的一致性已得到证实。酶的分子量已测定。这种酶被称为agavian。
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