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
Language English Country Netherlands Media print-electronic
Document type Evaluation Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
20828700
DOI
10.1016/j.chroma.2010.08.022
PII: S0021-9673(10)01074-5
Knihovny.cz E-resources
- MeSH
- Electrophoresis, Capillary methods MeSH
- Mass Spectrometry methods MeSH
- Protein Processing, Post-Translational MeSH
- Serum Albumin, Bovine chemistry MeSH
- Cattle MeSH
- Chromatography, High Pressure Liquid methods MeSH
- Animals MeSH
- Check Tag
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Evaluation Study MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Serum Albumin, Bovine MeSH
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) and capillary zone electrophoresis (CZE). Both of these methods used mass spectrometric (MS) detection. Three enzymes (trypsin, pepsin, proteinase K) were used to digest glycated BSA. The extent of modification depended on the selected oxo-compound. Reactivity increased progressively from glucose to glutardialdehyde (glucose
References provided by Crossref.org
Oxidation as an important factor of protein damage: Implications for Maillard reaction
