COMPARISON OF METHYL VIOLET INTERACTION WITH BOVINE SERUM ALBUMIN AND HUMAN SERUM ALBUMIN BY UV-DENATURATION METHOD

M. Shahinyan, M. Mikaelyan, M. Parsadanyan, A. Antonyan
{"title":"COMPARISON OF METHYL VIOLET INTERACTION WITH BOVINE SERUM ALBUMIN AND HUMAN SERUM ALBUMIN BY UV-DENATURATION METHOD","authors":"M. Shahinyan, M. Mikaelyan, M. Parsadanyan, A. Antonyan","doi":"10.46991/pysu:b/2022.56.2.136","DOIUrl":null,"url":null,"abstract":"In the present work the interaction of methyl violet (MV) with human serum albumin (HSA) and bovine serum albumin (BSA) has been studied by the UV-denaturation method and the obtained data were compared. The denaturation parameters – denaturation temperature and denaturation interval width, were determined. It was shown that MV, binding to serum albumins, stabilizes their structure. At the same time, the stabilization degree is different. It was also shown that BSA is stabilized more, than HSA, while binding to MV.","PeriodicalId":20692,"journal":{"name":"Proceedings of the YSU B: Chemical and Biological Sciences","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2022-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","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/2022.56.2.136","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

In the present work the interaction of methyl violet (MV) with human serum albumin (HSA) and bovine serum albumin (BSA) has been studied by the UV-denaturation method and the obtained data were compared. The denaturation parameters – denaturation temperature and denaturation interval width, were determined. It was shown that MV, binding to serum albumins, stabilizes their structure. At the same time, the stabilization degree is different. It was also shown that BSA is stabilized more, than HSA, while binding to MV.
用紫外变性法比较甲基紫与牛血清白蛋白和人血清白蛋白的相互作用
本文用紫外变性法研究了甲基紫(MV)与人血清白蛋白(HSA)和牛血清白蛋白(BSA)的相互作用,并对所得数据进行了比较。确定了变性参数——变性温度和变性区间宽度。结果表明,MV与血清白蛋白结合,稳定其结构。同时,稳定化程度不同。结果表明,在与MV结合时,BSA比HSA更稳定。
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