作者: Statis Pataridis , Zdeňka Štastná , Pavla Sedláková , Ivan Mikšík
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摘要: Post-translational modifications are significant reactions that occur to proteins. One of these is a non-enzymatic reaction between the oxo-group(s) sugars and amino-group(s) protein - glycation. This plays an important role in chronic complications diabetes mellitus, or aging process organisms, is, it has pathophysiology "normal" physiology animals. In work presented here, we studied glycation albumins (HSA BSA). Methodologically, used nano-LC coupled QTOF mass spectrometer. vitro-modified proteins were cleaved by trypsin arising peptides separated on C(18) nano column with trap-column. Peptides their analysed high-resolution spectrometer determination precision better than 5 ppm. Non-enzymatic vitro products albumin ribose identified. Besides well-known carboxymethyl lysine, new determined creating shifts 78 218. The origin first modification discussed its possible structure presented. addition, shift 132 belonging Schiff base was also location all within reactivity various oxo-compounds examined.