A differential scanning calorimetric study of the binding of sulfate ion and of Cibacron blue F3GA to yeast phosphoglycerate kinase.

A differential scanning calorimetric study of the binding of sulfate ion and of Cibacron blue F3GA to yeast phosphoglycerate kinase.
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硫酸根离子和 Cibacron 蓝 F3GA 与酵母磷酸甘油酸激酶结合的差示扫描量热研究。

DOI:
10.1021/bi00428a060
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发表时间:
1989
期刊:
影响因子:
2.9
通讯作者:
Sturtevant,JM
Sturtevant,JM
中科院分区:
生物学3区
文献类型:
--
作者:
Hu,CQ;Sturtevant,JM

文献摘要

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耶鲁大学化学系、分子生物物理学和生物化学系,纽黑文,康涅狄格州 06511 收稿日期:1988 年 4 月 26 日;修订稿于 1988 年 8 月 9 日收到 摘要:作为早期工作的延续 [Hu, CQ, & Sturtevant, J. M.(1987) Biochemistry 26,178-182],差示扫描量热法已被用于研究两种酶抑制剂、硫酸根离子和染料 Cibacron blue F3GA 对酵母磷酸甘油酸激酶热变性的影响。硫酸根离子,与在宿主蛋白解折叠过程中解离的配体一样,会提高 f1
Departments of Chemistry and of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511 Received April 26, 1988; Revised Manuscript Received August 9, 1988 abstract: In continuation of earlier work [Hu, CQ, & Sturtevant, J. M.(1987) Biochemistry 26,178-182], differential scanning calorimetry has been employed in a study of the effects on the thermal denaturation of yeast phosphoglycerate kinase of two inhibitors of the enzyme, sulfate ion and the dye Cibacron blue F3GA. Sulfate ion, as is usual with ligands that dissociate during unfoldingof thehost protein, raises f1