Expression and basic biochemical characteristics of recombinant surfactant protein D of bottlenose dolphin (Tursiops truncatus)

IF 1.4 4区 生物学 Q4 BIOCHEMICAL RESEARCH METHODS
Takahisa Hamano , Makio Yanagisawa , Seiji Hobo
{"title":"Expression and basic biochemical characteristics of recombinant surfactant protein D of bottlenose dolphin (Tursiops truncatus)","authors":"Takahisa Hamano ,&nbsp;Makio Yanagisawa ,&nbsp;Seiji Hobo","doi":"10.1016/j.pep.2024.106523","DOIUrl":null,"url":null,"abstract":"<div><p>We previously identified surfactant protein D (SP-D) in the bottlenose dolphin <em>Tursiops truncatus</em> as a unique evolutionary factor of the cetacean pulmonary immune system. In this short report, recombinant SP-D of bottlenose dolphin (dSP-D) was synthesized in mammalian cells, and its properties were analyzed <em>in vitro</em>. The recombinant proteins were purified using Ni-carrier or Co-carrier. Sodium dodecyl sulfate poly-acrylamide gel electrophoresis and western blotting revealed a 50 kDa major band with minor secondary bands. Enzyme-linked immunosorbent assay-like methods revealed that recombinant dSP-D bonded to gram-positive and gram-negative bacterial walls. Our findings suggest the clinical usefulness of dSP-D for cetacean pneumonia.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"222 ","pages":"Article 106523"},"PeriodicalIF":1.4000,"publicationDate":"2024-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Protein expression and purification","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1046592824000950","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}
引用次数: 0

Abstract

We previously identified surfactant protein D (SP-D) in the bottlenose dolphin Tursiops truncatus as a unique evolutionary factor of the cetacean pulmonary immune system. In this short report, recombinant SP-D of bottlenose dolphin (dSP-D) was synthesized in mammalian cells, and its properties were analyzed in vitro. The recombinant proteins were purified using Ni-carrier or Co-carrier. Sodium dodecyl sulfate poly-acrylamide gel electrophoresis and western blotting revealed a 50 kDa major band with minor secondary bands. Enzyme-linked immunosorbent assay-like methods revealed that recombinant dSP-D bonded to gram-positive and gram-negative bacterial walls. Our findings suggest the clinical usefulness of dSP-D for cetacean pneumonia.

瓶鼻海豚(Tursiops truncatus)重组表面活性蛋白 D 的表达和基本生化特征。
我们曾在瓶鼻海豚(Tursiops truncatus)中发现表面活性蛋白 D(SP-D)是鲸类肺部免疫系统的独特进化因子。在这篇简短的报告中,我们在哺乳动物细胞中合成了瓶鼻海豚的重组 SP-D(dSP-D),并在体外分析了其特性。使用镍载体或共载体纯化了重组蛋白。十二烷基硫酸钠聚丙烯酰胺凝胶电泳和 Western 印迹显示了一个 50 kDa 的主要条带和次要条带。类似酶联免疫吸附试验的方法显示,重组 dSP-D 与革兰氏阳性和革兰氏阴性细菌的菌壁结合。我们的研究结果表明,dSP-D 可用于鲸目动物肺炎的临床治疗。
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
Protein expression and purification
Protein expression and purification 生物-生化研究方法
CiteScore
3.70
自引率
6.20%
发文量
120
审稿时长
32 days
期刊介绍: Protein Expression and Purification is an international journal providing a forum for the dissemination of new information on protein expression, extraction, purification, characterization, and/or applications using conventional biochemical and/or modern molecular biological approaches and methods, which are of broad interest to the field. The journal does not typically publish repetitive examples of protein expression and purification involving standard, well-established, methods. However, exceptions might include studies on important and/or difficult to express and/or purify proteins and/or studies that include extensive protein characterization, which provide new, previously unpublished information.
×
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