尤利西斯反转录转座子天冬氨酸蛋白酶(果蝇)。

Voprosy meditsinskoi khimii Pub Date : 2002-11-01
D A Volkov, L V Savvateeva, N I Dergousova, L D Rumsh
{"title":"尤利西斯反转录转座子天冬氨酸蛋白酶(果蝇)。","authors":"D A Volkov,&nbsp;L V Savvateeva,&nbsp;N I Dergousova,&nbsp;L D Rumsh","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Retrotransposones are mobile genetic elements occurring in genomes of bacteria, plants or animals. Retrotransposones were found to contain nucleotide sequences encoding proteins which are homological to retroviral aspartic proteinases. Our research has been focused on Ulysses which is mobile genetic element found in Drosophila virilis. We suggested a primary structure of Ulysses proteinase using comparative analysis of amino acid sequences of retroviral proteinases and proteinases from retrotransposones. The appropriate cDNA fragment has been cloned and expressed in E. coli. The purification of recombinant protein (12 kD) has been carried out by affinity chromatography using pepstatine-agarose. The obtained protein has proteolytic activity at optimum pH 5.5 like the majority of aspartic proteinases.</p>","PeriodicalId":23535,"journal":{"name":"Voprosy meditsinskoi khimii","volume":"48 6","pages":"553-60"},"PeriodicalIF":0.0000,"publicationDate":"2002-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Ulysses retrotransposon aspartate proteinase (Drosophila virilis)].\",\"authors\":\"D A Volkov,&nbsp;L V Savvateeva,&nbsp;N I Dergousova,&nbsp;L D Rumsh\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Retrotransposones are mobile genetic elements occurring in genomes of bacteria, plants or animals. Retrotransposones were found to contain nucleotide sequences encoding proteins which are homological to retroviral aspartic proteinases. Our research has been focused on Ulysses which is mobile genetic element found in Drosophila virilis. We suggested a primary structure of Ulysses proteinase using comparative analysis of amino acid sequences of retroviral proteinases and proteinases from retrotransposones. The appropriate cDNA fragment has been cloned and expressed in E. coli. The purification of recombinant protein (12 kD) has been carried out by affinity chromatography using pepstatine-agarose. The obtained protein has proteolytic activity at optimum pH 5.5 like the majority of aspartic proteinases.</p>\",\"PeriodicalId\":23535,\"journal\":{\"name\":\"Voprosy meditsinskoi khimii\",\"volume\":\"48 6\",\"pages\":\"553-60\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2002-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Voprosy meditsinskoi khimii\",\"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":"Voprosy meditsinskoi khimii","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

反转录转座子是存在于细菌、植物或动物基因组中的可移动遗传元件。发现反转录转座子含有与逆转录天冬氨酸蛋白酶同源的核苷酸序列。我们的研究重点是在果蝇中发现的移动遗传因子尤利西斯(Ulysses)。我们通过对逆转录病毒蛋白酶和反转录转座子蛋白酶的氨基酸序列的比较分析,提出了Ulysses蛋白酶的一级结构。已克隆出相应的cDNA片段,并在大肠杆菌中表达。重组蛋白(12kd)采用胃泌素-琼脂糖亲和层析纯化。所得蛋白与大多数天冬氨酸蛋白酶一样,在最适pH为5.5时具有蛋白水解活性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
[Ulysses retrotransposon aspartate proteinase (Drosophila virilis)].

Retrotransposones are mobile genetic elements occurring in genomes of bacteria, plants or animals. Retrotransposones were found to contain nucleotide sequences encoding proteins which are homological to retroviral aspartic proteinases. Our research has been focused on Ulysses which is mobile genetic element found in Drosophila virilis. We suggested a primary structure of Ulysses proteinase using comparative analysis of amino acid sequences of retroviral proteinases and proteinases from retrotransposones. The appropriate cDNA fragment has been cloned and expressed in E. coli. The purification of recombinant protein (12 kD) has been carried out by affinity chromatography using pepstatine-agarose. The obtained protein has proteolytic activity at optimum pH 5.5 like the majority of aspartic proteinases.

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
[Hydrolysis by enteropeptidase of nonspecific (model) peptide sequences and possible physiological role of this phenomenon]. [Ulysses retrotransposon aspartate proteinase (Drosophila virilis)]. [Polymer coatings with immobilized thrombin and peptides: preparation and use for wound healing]. [Isolation, purification, and properties of factor XII and its active fragment (beta-XIIa)]. [Tripeptidyl peptidase 1 deficiency in neuronal ceroid lipofuscinosis. A novel mutation].
×
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