Effect of phosphate concentration on the kinetics of bovine liver glutamate dehydrogenase self-association

Ryoichi Tashiro, Akie Nishimura, Tohru Inoue, Ryosuke Shimozawa
{"title":"Effect of phosphate concentration on the kinetics of bovine liver glutamate dehydrogenase self-association","authors":"Ryoichi Tashiro,&nbsp;Akie Nishimura,&nbsp;Tohru Inoue,&nbsp;Ryosuke Shimozawa","doi":"10.1016/0005-2795(81)90087-8","DOIUrl":null,"url":null,"abstract":"<div><p>The kinetics of the self-association of bovine liver glutamate dehydrogenase was studied at various phosphate buffer concentrations (pH 7.3) at 11.5°C by means of the temperature-jump technique with scattered light detection. The observed relaxation times were well explained by the random association model of Thusius et al. With increasing phosphate concentration, the association rate constant derived from the model decreased, while the dissociation rate constant was left almost constant. Relaxation amplitude was also dependent on the phosphate concentration. The changes in the rate constant and relaxation amplitude with phosphate concentration are well elucidated by assuming that glutamate dehydrogenase is protected from association by specific masking of the association site by phosphate ions.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"671 1","pages":"Pages 9-15"},"PeriodicalIF":0.0000,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90087-8","citationCount":"5","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005279581900878","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 5

Abstract

The kinetics of the self-association of bovine liver glutamate dehydrogenase was studied at various phosphate buffer concentrations (pH 7.3) at 11.5°C by means of the temperature-jump technique with scattered light detection. The observed relaxation times were well explained by the random association model of Thusius et al. With increasing phosphate concentration, the association rate constant derived from the model decreased, while the dissociation rate constant was left almost constant. Relaxation amplitude was also dependent on the phosphate concentration. The changes in the rate constant and relaxation amplitude with phosphate concentration are well elucidated by assuming that glutamate dehydrogenase is protected from association by specific masking of the association site by phosphate ions.

磷酸盐浓度对牛肝谷氨酸脱氢酶自结合动力学的影响
采用跳温散射光检测技术,在11.5℃条件下,研究了不同磷酸盐缓冲液浓度(pH 7.3)下牛肝谷氨酸脱氢酶的自结合动力学。观察到的松弛时间可以用Thusius等人的随机关联模型很好地解释。随着磷酸盐浓度的增加,模型得到的缔合速率常数减小,而解离速率常数基本保持不变。松弛幅度也依赖于磷酸盐浓度。速率常数和弛豫振幅随磷酸盐浓度的变化可以很好地解释,假设谷氨酸脱氢酶通过磷酸盐离子特异性掩蔽结合位点来保护其不发生结合。
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