Albumin-bound low molecular weight thiols analysis in plasma and carotid plaques by CE

We describe a new method for the quantification of low molecular weight thiols, as homocysteine, cysteine, cysteinylglycine, glutamylcysteine and glutathione bound to human plasma albumin. After albumin isolation and purification by SDS-PAGE, thiols were freed from protein with tri-n-butylphosphine...

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Bibliographic Details
Published in:Journal of separation science 2010, Vol.33 (1), p.126-131
Main Authors: Zinellu, Angelo, Lepedda, Antonio, Sotgia, Salvatore, Zinellu, Elisabetta, Marongiu, Giommaria, Usai, Maria Franca, Gaspa, Leonardo, De Muro, Pierina, Formato, Marilena, Deiana, Luca, Carru, Ciriaco
Format: Article
Language:English
Subjects:
Albumin
Albumins
Albumins - chemistry
Albumins - metabolism
Carotid Stenosis
Cysteine
Electrophoresis, Capillary - methods
Electrophoresis, Polyacrylamide Gel - methods
Elevated
Fluoresceins - chemistry
Homocysteine
Human
Humans
Limit of Detection
Low molecular weights
Migration
Molecular Weight
Purification
Reproducibility
SDS-PAGE
Sulfhydryl Compounds - blood
Sulfhydryl Compounds - chemistry
Thiols
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Summary:We describe a new method for the quantification of low molecular weight thiols, as homocysteine, cysteine, cysteinylglycine, glutamylcysteine and glutathione bound to human plasma albumin. After albumin isolation and purification by SDS-PAGE, thiols were freed from protein with tri-n-butylphosphine and successively derivatized with 5-iodoacetamidofluorescein. Samples were then injected and quantified in about 18 min by CE with laser induced fluorescence detection. Precision tests indicate a good repeatability of the method both for migration times (RSD
ISSN:1615-9306
1615-9314
DOI:10.1002/jssc.200900582