牛腮腺胱抑素C的特性:半胱氨酸蛋白酶抑制和抗病毒特性。

N Cimerman, M D Kosorok, B D Korant, B Turk, V Turk
{"title":"牛腮腺胱抑素C的特性:半胱氨酸蛋白酶抑制和抗病毒特性。","authors":"N Cimerman,&nbsp;M D Kosorok,&nbsp;B D Korant,&nbsp;B Turk,&nbsp;V Turk","doi":"10.1515/bchm3.1996.377.1.19","DOIUrl":null,"url":null,"abstract":"<p><p>Cystatin C, a low Mr cysteine proteinase inhibitor was isolated from bovine parotid glands by a procedure which includes alkaline treatment of the homogenate, affinity chromatography, gel filtration and ion exchange chromatography. The purified inhibitor has a pl of 8.0 and Mr of 14500. The identity with bovine cystatin C from colostrum was confirmed by N-terminal sequence of the inhibitor and amino acid composition. Cystatin C rapidly (kass = 5.5 x 10(7) M-1s-1) and tightly inhibits papain (Ki = 0.02 nM), whereas its interaction with bovine cathepsin B is substantially weaker (Ki = 4.4 nM). Bovine cystatin C also shows a weak antiviral effect on poliovirus infected human Hela cells.</p>","PeriodicalId":8963,"journal":{"name":"Biological chemistry Hoppe-Seyler","volume":"377 1","pages":"19-23"},"PeriodicalIF":0.0000,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm3.1996.377.1.19","citationCount":"21","resultStr":"{\"title\":\"Characterization of cystatin C from bovine parotid glands: cysteine proteinase inhibition and antiviral properties.\",\"authors\":\"N Cimerman,&nbsp;M D Kosorok,&nbsp;B D Korant,&nbsp;B Turk,&nbsp;V Turk\",\"doi\":\"10.1515/bchm3.1996.377.1.19\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Cystatin C, a low Mr cysteine proteinase inhibitor was isolated from bovine parotid glands by a procedure which includes alkaline treatment of the homogenate, affinity chromatography, gel filtration and ion exchange chromatography. The purified inhibitor has a pl of 8.0 and Mr of 14500. The identity with bovine cystatin C from colostrum was confirmed by N-terminal sequence of the inhibitor and amino acid composition. Cystatin C rapidly (kass = 5.5 x 10(7) M-1s-1) and tightly inhibits papain (Ki = 0.02 nM), whereas its interaction with bovine cathepsin B is substantially weaker (Ki = 4.4 nM). Bovine cystatin C also shows a weak antiviral effect on poliovirus infected human Hela cells.</p>\",\"PeriodicalId\":8963,\"journal\":{\"name\":\"Biological chemistry Hoppe-Seyler\",\"volume\":\"377 1\",\"pages\":\"19-23\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1996-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1515/bchm3.1996.377.1.19\",\"citationCount\":\"21\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biological chemistry Hoppe-Seyler\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1515/bchm3.1996.377.1.19\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biological chemistry Hoppe-Seyler","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1515/bchm3.1996.377.1.19","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 21

摘要

半胱氨酸蛋白酶抑制剂Cystatin C是一种低Mr半胱氨酸蛋白酶抑制剂,经匀浆碱性处理、亲和层析、凝胶过滤和离子交换层析从牛腮腺中分离得到。纯化后的抑制剂的pl为8.0,Mr为14500。该抑制剂的n端序列和氨基酸组成证实其与牛初乳胱抑素C同源。胱抑素C快速抑制木瓜蛋白酶(kass = 5.5 × 10(7) M-1s-1),并紧密抑制木瓜蛋白酶(Ki = 0.02 nM),而与牛组织蛋白酶B的相互作用则弱得多(Ki = 4.4 nM)。牛胱抑素C对脊髓灰质炎病毒感染的人Hela细胞也显示出微弱的抗病毒作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Characterization of cystatin C from bovine parotid glands: cysteine proteinase inhibition and antiviral properties.

Cystatin C, a low Mr cysteine proteinase inhibitor was isolated from bovine parotid glands by a procedure which includes alkaline treatment of the homogenate, affinity chromatography, gel filtration and ion exchange chromatography. The purified inhibitor has a pl of 8.0 and Mr of 14500. The identity with bovine cystatin C from colostrum was confirmed by N-terminal sequence of the inhibitor and amino acid composition. Cystatin C rapidly (kass = 5.5 x 10(7) M-1s-1) and tightly inhibits papain (Ki = 0.02 nM), whereas its interaction with bovine cathepsin B is substantially weaker (Ki = 4.4 nM). Bovine cystatin C also shows a weak antiviral effect on poliovirus infected human Hela cells.

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
×
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
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
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 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信