BOVINE SERUM ALBUMIN DENATURATION IN THE PRESENCE OF HOECHST 33258 AND METHYLENE BLUE

P. O. Vardevanyan, M. Mikaelyan, N. Petrosyan
{"title":"BOVINE SERUM ALBUMIN DENATURATION IN THE PRESENCE OF HOECHST 33258 AND METHYLENE BLUE","authors":"P. O. Vardevanyan, M. Mikaelyan, N. Petrosyan","doi":"10.46991/PYSU:B/2020.54.3.204","DOIUrl":null,"url":null,"abstract":"The interaction of Hoechst 33258 (H33258) and methylene blue (MB) compounds with bovine serum albumin (BSA) has been studied using the method of thermal denaturation. The obtained data showed that both ligands form complexes with BSA, moreover, MB binds to BSA stronger than H33258. Furthermore, H33258 destabilizes, while MB stabilizes the native structure of protein, leading to the decrease and increase of the denaturation temperature of BSA respectively.","PeriodicalId":20692,"journal":{"name":"Proceedings of the YSU B: Chemical and Biological Sciences","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2020-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Proceedings of the YSU B: Chemical and Biological Sciences","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.46991/PYSU:B/2020.54.3.204","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1

Abstract

The interaction of Hoechst 33258 (H33258) and methylene blue (MB) compounds with bovine serum albumin (BSA) has been studied using the method of thermal denaturation. The obtained data showed that both ligands form complexes with BSA, moreover, MB binds to BSA stronger than H33258. Furthermore, H33258 destabilizes, while MB stabilizes the native structure of protein, leading to the decrease and increase of the denaturation temperature of BSA respectively.
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
牛血清白蛋白变性在hoechst 33258和亚甲基蓝存在
采用热变性法研究了Hoechst 33258 (H33258)和亚甲基蓝(MB)化合物与牛血清白蛋白(BSA)的相互作用。结果表明,两种配体均能与BSA形成配合物,且MB对BSA的结合强于H33258。H33258使蛋白失稳,MB使蛋白的天然结构稳定,分别导致牛血清蛋白变性温度的降低和升高。
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 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
QUANTUM CHEMICAL CALCULATION OF STRUCTURAL AND THERMODYNAMIC PROPERTIES OF ETHYL METHYL SULFONE IN THE GAS PHASE SPECTROPHOTOMETRIC STUDY OF COMPLEXES OF SOME INTERCALATORS WITH DOUBLE-STRANDED AND SINGLE-STRANDED NUCLEIC ACIDS BIOMASS FORMATION BY DIFFERENT COLLECTIONS OF $PLEUROTUS$ SPP. DURING SUBMERGED GROWTH CONDUCTIVE POLYMERS AS MATERIALS USED IN SENSORS FOR DETERMINATION OF IMPORTANT VOLATILE COMPOUNDS IN THE FIELD OF FOOD SAFETY STUDY OF ANTIOXIDANT PROPERTIES OF SOME TYPES OF PACKAGED COFFEE
×
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