A rapid simplified purification of bovine thrombin.

Z Ding, Y Xu
{"title":"A rapid simplified purification of bovine thrombin.","authors":"Z Ding,&nbsp;Y Xu","doi":"10.1080/10826069508010105","DOIUrl":null,"url":null,"abstract":"<p><p>A rapid simplified method was developed to obtain highly pure bovine thrombin. Prothrombin was directly activated when it was enriched from bovine plasma without prior purification. The activated thrombin was isolated by a single Heparin-Sepharose affinity chromatography step. About 87% of activated thrombin was recovered and the yield was 25.1 mg of thrombin per liter of starting plasma. Specific activity of the final preparation was 4018 NIH units/mg, representing a 402 fold purification over the starting material. Comparative experiments showed that the simplified method was about six times as effective as previous two-step methods.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"25 1-2","pages":"21-8"},"PeriodicalIF":0.0000,"publicationDate":"1995-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069508010105","citationCount":"10","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Preparative biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/10826069508010105","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 10

Abstract

A rapid simplified method was developed to obtain highly pure bovine thrombin. Prothrombin was directly activated when it was enriched from bovine plasma without prior purification. The activated thrombin was isolated by a single Heparin-Sepharose affinity chromatography step. About 87% of activated thrombin was recovered and the yield was 25.1 mg of thrombin per liter of starting plasma. Specific activity of the final preparation was 4018 NIH units/mg, representing a 402 fold purification over the starting material. Comparative experiments showed that the simplified method was about six times as effective as previous two-step methods.

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
牛凝血酶的快速简化纯化。
建立了一种获得高纯度牛凝血酶的快速简化方法。当从牛血浆中富集凝血酶原而无需事先纯化时,凝血酶原被直接激活。活化凝血酶通过肝素- sepharose亲和层析分离得到。活化凝血酶回收率约为87%,每升起始血浆凝血酶产率为25.1 mg。最终制备的比活性为4018 NIH单位/mg,比起始材料纯化402倍。对比实验表明,该简化方法的效率是之前两步法的6倍左右。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
A rapid method for the isolation of genomic DNA from Aspergillus fumigatus. Purification of chlorpromazine-sensitive GTPase from rat cerebral cortex. Evaluation of a purification procedure for the muscarinic receptor for the purpose of quantitative receptor assays of anticholinergics. Part A: The membrane-bound receptor. Evaluation of a purification procedure for the muscarinic receptor for the purpose of quantitative receptor assays of anticholinergics. Part B: The solubilized receptor. Purification and characterization of rat parotid glycosylated, basic and acidic proline-rich proteins.
×
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