Protein folding observed by capillary electrophoresis in isoelectric buffers

被引：28

作者：

Stellwagen, E ^{[1
]}

Gelfi, C

Righetti, PG

机构：

[1] Univ Iowa, Dept Biochem, Iowa City, IA 52242 USA

[2] CNR, Ist Tecnol Biomed Avanzate, I-20090 Milan, Italy

[3] Univ Verona, Dept Agr & Ind Biotechnol, I-37134 Verona, Italy

来源：

JOURNAL OF CHROMATOGRAPHY A | 1999年 / 838卷 / 1-2期

关键词：

protein folding; buffer composition; proteins; cytochromes;

D O I：

10.1016/S0021-9673(98)01048-6

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Capillary zone electrophoresis measurements in acidic isoelectric buffers provide a sensitive and rapid method for comparison of the folding and stability of wild type, mutant or post-translationally modified proteins. The potential of the method is illustrated using the small globular protein cytochrome c. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：131 / 138

页数：8

共 7 条

[1] PARTICIPATION OF PROTEIN LIGANDS IN FOLDING OF CYTOCHROME C [J].