Journal
JOURNAL OF CHROMATOGRAPHY A
Volume 1217, Issue 51, Pages 8009-8015Publisher
ELSEVIER
DOI: 10.1016/j.chroma.2010.08.022
Keywords
Glycation; Albumin; HPLC-MS; CE-MS
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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. (C) 2010 Elsevier B.V. All rights reserved.
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