Nucleotide sequence of cDNA for porcine heme oxygenase and its expression in Escherichia coli.

Biochemistry international Pub Date : 1992-12-01
T Suzuki, M Sato, K Ishikawa, T Yoshida
{"title":"Nucleotide sequence of cDNA for porcine heme oxygenase and its expression in Escherichia coli.","authors":"T Suzuki,&nbsp;M Sato,&nbsp;K Ishikawa,&nbsp;T Yoshida","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The nucleotide sequence of a cDNA for porcine heme oxygenase was determined. The open reading frame encoded a polypeptide of 288 amino acid residues with a molecular mass of 33,074 Da. A prokaryotic expression plasmid carrying porcine heme oxygenase cDNA was constructed and transfected into Escherichia coli cells. The full-length heme oxygenase expressed was localized in the bacterial membranes. Two small-sized heme oxygenases with no membrane-bound properties were also detected, suggesting that in E. coli cells a considerable amount of the enzyme expressed was degraded.</p>","PeriodicalId":8778,"journal":{"name":"Biochemistry international","volume":"28 5","pages":"887-93"},"PeriodicalIF":0.0000,"publicationDate":"1992-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemistry international","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

Abstract

The nucleotide sequence of a cDNA for porcine heme oxygenase was determined. The open reading frame encoded a polypeptide of 288 amino acid residues with a molecular mass of 33,074 Da. A prokaryotic expression plasmid carrying porcine heme oxygenase cDNA was constructed and transfected into Escherichia coli cells. The full-length heme oxygenase expressed was localized in the bacterial membranes. Two small-sized heme oxygenases with no membrane-bound properties were also detected, suggesting that in E. coli cells a considerable amount of the enzyme expressed was degraded.

猪血红素加氧酶cDNA核苷酸序列及其在大肠杆菌中的表达。
测定了猪血红素加氧酶cDNA的核苷酸序列。开放阅读框编码288个氨基酸残基的多肽,分子量为33,074 Da。构建了猪血红素加氧酶cDNA原核表达质粒,并将其转染大肠杆菌细胞。表达的全长血红素加氧酶定位在细菌膜上。两种没有膜结合特性的小尺寸血红素加氧酶也被检测到,这表明在大肠杆菌细胞中,大量表达的酶被降解。
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 求助全文
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