蛇毒素:结构与功能。

Journal of natural toxins Pub Date : 1999-06-01
C C Yang
{"title":"蛇毒素:结构与功能。","authors":"C C Yang","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Cobrotoxin is the main neurotoxic protein isolated from the venom of Taiwan cobra Naja naja atra. It is a small, basic protein consisting of a single polypeptide chain of 62 amino acids, cross-linked by four disulfide bonds. The disulfide bonds and Tyr-25 which is buried in the molecule form a central core to maintain and stabilize the active conformation of the toxin. Selective and stepwise chemical modifications of cobrotoxin indicate that at least two cationic groups, an epsilon-amino group of Lys-47 and a guanidino group of Arg-33, both of which are common to all known postsynaptic neurotoxins, held at a certain critical distance in the molecule, are functionally important for its neuromuscular blocking activity. The cDNA encoding cobrotoxin was constructed from the cellular RNA isolated from the venom glands of Naja naja atra by reverse transcription polymerase chain reaction. Sequencing several clones containing about 0.5 Kb DNA inserts contained a complete and full-length reading frame of 249 base pairs covering a precursor of cobrotoxin gene with a deduced mature protein sequence of 62 amino acids which are identical to the amino acid sequence of cobrotoxin and a 21 amino acid segment of signal peptide. Expression of cobrotoxin in E. coli vector generated a polypeptide which can cross-react with the antisera against the native cobrotoxin.</p>","PeriodicalId":16437,"journal":{"name":"Journal of natural toxins","volume":"8 2","pages":"221-33"},"PeriodicalIF":0.0000,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Cobrotoxin: structure and function.\",\"authors\":\"C C Yang\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Cobrotoxin is the main neurotoxic protein isolated from the venom of Taiwan cobra Naja naja atra. It is a small, basic protein consisting of a single polypeptide chain of 62 amino acids, cross-linked by four disulfide bonds. The disulfide bonds and Tyr-25 which is buried in the molecule form a central core to maintain and stabilize the active conformation of the toxin. Selective and stepwise chemical modifications of cobrotoxin indicate that at least two cationic groups, an epsilon-amino group of Lys-47 and a guanidino group of Arg-33, both of which are common to all known postsynaptic neurotoxins, held at a certain critical distance in the molecule, are functionally important for its neuromuscular blocking activity. The cDNA encoding cobrotoxin was constructed from the cellular RNA isolated from the venom glands of Naja naja atra by reverse transcription polymerase chain reaction. Sequencing several clones containing about 0.5 Kb DNA inserts contained a complete and full-length reading frame of 249 base pairs covering a precursor of cobrotoxin gene with a deduced mature protein sequence of 62 amino acids which are identical to the amino acid sequence of cobrotoxin and a 21 amino acid segment of signal peptide. Expression of cobrotoxin in E. coli vector generated a polypeptide which can cross-react with the antisera against the native cobrotoxin.</p>\",\"PeriodicalId\":16437,\"journal\":{\"name\":\"Journal of natural toxins\",\"volume\":\"8 2\",\"pages\":\"221-33\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1999-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of natural toxins\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of natural toxins","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

摘要

蛇毒素是从台湾眼镜蛇的毒液中分离出来的主要神经毒性蛋白。它是一种小的碱性蛋白质,由62个氨基酸组成的单肽链,由四个二硫键交联。二硫键和埋藏在分子中的tyr25形成了一个中心核心,以维持和稳定毒素的活性构象。蛇毒素的选择性和逐步化学修饰表明,至少有两个阳离子基团(Lys-47的ε -氨基和Arg-33的胍基)在分子中保持一定的临界距离,对其神经肌肉阻断活性起重要作用。利用逆转录聚合酶链反应,从大白鲨毒腺中分离到编码蛇毒素的细胞RNA,构建了编码蛇毒素的cDNA。对含有约0.5 Kb DNA插入片段的多个克隆进行测序,得到了覆盖蛇毒基因前体的249个碱基对的完整全长阅读框,推断出与蛇毒基因相同的62个氨基酸的成熟蛋白序列和21个氨基酸的信号肽片段。在大肠杆菌载体中表达蛇毒素,产生一种多肽,该多肽能与天然蛇毒素的抗血清发生交叉反应。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Cobrotoxin: structure and function.

Cobrotoxin is the main neurotoxic protein isolated from the venom of Taiwan cobra Naja naja atra. It is a small, basic protein consisting of a single polypeptide chain of 62 amino acids, cross-linked by four disulfide bonds. The disulfide bonds and Tyr-25 which is buried in the molecule form a central core to maintain and stabilize the active conformation of the toxin. Selective and stepwise chemical modifications of cobrotoxin indicate that at least two cationic groups, an epsilon-amino group of Lys-47 and a guanidino group of Arg-33, both of which are common to all known postsynaptic neurotoxins, held at a certain critical distance in the molecule, are functionally important for its neuromuscular blocking activity. The cDNA encoding cobrotoxin was constructed from the cellular RNA isolated from the venom glands of Naja naja atra by reverse transcription polymerase chain reaction. Sequencing several clones containing about 0.5 Kb DNA inserts contained a complete and full-length reading frame of 249 base pairs covering a precursor of cobrotoxin gene with a deduced mature protein sequence of 62 amino acids which are identical to the amino acid sequence of cobrotoxin and a 21 amino acid segment of signal peptide. Expression of cobrotoxin in E. coli vector generated a polypeptide which can cross-react with the antisera against the native cobrotoxin.

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