Evaluation of acid hydrolysis of proteins on Se-aminoacids and trimethylselenonium species by liquid chromatography-microwave digestion hydride generation-atomic absorption spectrometry

Citation
Ma. Palacios et al., Evaluation of acid hydrolysis of proteins on Se-aminoacids and trimethylselenonium species by liquid chromatography-microwave digestion hydride generation-atomic absorption spectrometry, QUIM ANAL, 18(2), 1999, pp. 163-168
Citations number
15
Categorie Soggetti
Spectroscopy /Instrumentation/Analytical Sciences
Journal title
QUIMICA ANALITICA
ISSN journal
02120569 → ACNP
Volume
18
Issue
2
Year of publication
1999
Pages
163 - 168
Database
ISI
SICI code
0212-0569(1999)18:2<163:EOAHOP>2.0.ZU;2-8
Abstract
A hyphenated on-line system consisting of an anion-exchange chromatographic column for species separation, a focussed microwave oven for species conve rsion to selenite, a hydride generation system for the derivatization of se lenite to selenium hydride and an atomic absorption spectrophotometry detec tor (HPLC-MO-HG-AAS) was used to evaluate selenomethionine, selenocystine a nd trimethylselenonium ion stability under acid hydrolysis treatment of pro tein. SeCys behaviour in the HPLC system remained unaltered. SeMet in the p resence of oxygen was completely decomposed; however, when oxidation with p erformic acid was carried out before hydrolysis, this species derivatized t o more highly oxidized and stable forms in a similar fashion to methionine. TMSe+ ion was practically completely decomposed by this treatment.