title: 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.
abstract: 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<ribose<glyoxal<glutardialdehyde). Carboxymethylation of lysine (CML) was the main type of modification detected. The HPLC/MS method achieved higher coverage and a larger amount of CML was identified compared to CZE/MS.
authors.affiliation: Institute of Physiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, 142 20 Prague 4, Czech Republic.
authors.forename: Zdeňka
authors.initials: Z
authors.lastname: Zmatliková
authors.forename: Pavla
authors.initials: P
authors.lastname: Sedláková
authors.forename: Katerina
authors.initials: K
authors.lastname: Lacinová
authors.forename: Adam
authors.initials: A
authors.lastname: Eckhardt
authors.forename: Statis
authors.initials: S
authors.lastname: Pataridis
authors.forename: Ivan
authors.initials: I
authors.lastname: Mikšík
mesh_terms: D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D019075:Electrophoresis, Capillary / Q000379:methods*; D013058:Mass Spectrometry / Q000379:methods*; D011499:Protein Processing, Post-Translational; D012710:Serum Albumin, Bovine / Q000737:chemistry*
chemical_list: D012710:Serum Albumin, Bovine