{"title":"又是一种新的植物蛋白酶","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":"{\"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}","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

摘要

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。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Agavain: A new plant proteinase

  • 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.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Subject index Erratum Erratum Author index Cation requirements for the acetic thiokinase from yeast
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1