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