Separation of glutathione and its novel analogues and determination of their dissociation constants by capillary electrophoresis

被引：7

作者：

Kazarjan, Jana ^{[1
]}

Vaher, Merike ^{[1
]}

Mahlapuu, Riina ^{[2
]}

Hansen, Mats ^{[2
]}

Soomets, Ursel ^{[2
]}

Kaljurand, Mihkel ^{[1
]}

机构：

[1] Tallinn Univ Technol, Dept Chem, EE-12618 Tallinn, Estonia

[2] Univ Tartu, Dept Biochem, Fac Med, Ctr Excellence Translat Med, EE-50090 Tartu, Estonia

来源：

ELECTROPHORESIS | 2013年 / 34卷 / 12期

关键词：

Capillary electrophoresis; pKa Determination; Separation of GSH analogues; LIQUID-CHROMATOGRAPHY; REDOX; CELL; PREDICTION; PEPTIDES; BEHAVIOR;

D O I：

10.1002/elps.201200611

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A CE protocol was developed to separate reduced glutathione and its four novel analogues UPF1 (Tyr(Me)--Glu-Cys-Gly), UPF17 (Tyr(Me)--Glu-Cys-Gly), UPF50 (-Ala-His-Tyr(Me)--Glu-Cys-Gly), and UPF51 (-Ala-His-Tyr(Me)--Glu-Cys-Gly), and their homo- and heterodimers by varying the ionic strength and/or pH of different BGEs. For the determination of dissociation constants (pKa) of the above-mentioned peptides the CE method was used. Effective electrophoretic mobilities of analytes were measured in the pH range 5.50-10.00 using optimized BGE with an ionic strength of 50 mM at 25 degrees C. pKa values were calculated by fitting the experimental points to a suitable model with correlation coefficients higher than 0.99. The pKa values for imidazolyl, amino and thiol moieties of the analyzed peptides were in the range 5.94-6.29, 8.81-9.10, and 7.86-8.13, respectively.

引用

页码：1820 / 1827

页数：8

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