RESUMO
A facile and convergent procedure for the synthesis of azobenzene-based probe was reported, which could selectively release interested proteins conducted with sodium dithionite. Besides, the cleavage efficiency is closely associated with the structural features, in which an ortho-hydroxyl substituent is necessary for reactivity. In addition, the azobenzene tag applied in the Ac4GlcNAz-labled proteins demonstrated high efficiency and selectivity in comparison with Biotin-PEG4-Alkyne, which provides a useful platform for enrichment of any desired bioorthogonal proteomics.
Assuntos
Acetilglucosamina/metabolismo , Alcinos/metabolismo , Azidas/metabolismo , Ditionita/metabolismo , N-Acetilglucosaminiltransferases/metabolismo , Acetilglucosamina/química , Alcinos/química , Azidas/química , Reação de Cicloadição , Ditionita/síntese química , Ditionita/química , Estrutura Molecular , N-Acetilglucosaminiltransferases/química , ProteômicaRESUMO
An ion chromatographic method for simultaneous determination of formate, hydroxyethyl sulfonate (HES), hydroxyethyl thiosulfate (HET), and coexisting anions in the industrial waste liquid of sodium hydrosulfite production was developed. The mixture of 1.6 mmol/l of phthalic acid and 1.2 mmol/l tri-(hydroxyethyl) aminomethane was used as eluent. The interference of coexisting sulfite anion with HES was avoided by selective oxidation with hydrogen peroxide as oxidizer. The other coexisting inorganic anions, Cl-, SO4(2-) and S2O3(2-) can be determined simultaneously. The linear range of the peak area calibration curves for all analytes was up to two or three orders of magnitude. The detection limits (S/N = 3) for formate, HES and HET were 2.4, 1.0 and 0.5 mg/l, respectively. The recoveries for all analytes were 91.61-100.6%.
