Non-enzymatic posttranslational modifications of bovine serum albumin by oxo-compounds investigated by high-performance liquid chromatography-mass spectrometry and capillary zone electrophoresis-mass spectrometry.
作者： Zdeňka Zmatliková , Pavla Sedláková , Katerina Lacinová , Adam Eckhardt , Statis Pataridis
DOI: 10.1016/J.CHROMA.2010.08.022
关键词: Chemistry 、 Bovine serum albumin 、 High-performance liquid chromatography 、 Glyoxal 、 Serum albumin 、 Capillary electrophoresis 、 Chromatography 、 Liquid chromatography–mass spectrometry 、 Trypsin 、 Mass spectrometry
摘要: Non-enzymatic posttranslational modifications of bovine serum albumin (BSA) by various oxo-compounds (glucose, ribose, glyoxal and glutardialdehyde) have been investigated using high-performance liquid chromatography (HPLC) capillary zone electrophoresis (CZE). Both these methods used mass spectrometric (MS) detection. Three enzymes (trypsin, pepsin, proteinase K) were to digest glycated BSA. The extent modification depended on the selected oxo-compound. Reactivity increased progressively from glucose glutardialdehyde (glucose < ribose glutardialdehyde). Carboxymethylation lysine (CML) was main type detected. HPLC/MS method achieved higher coverage a larger amount CML identified compared CZE/MS.
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