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• W2023387648 abstract "Carbamylation is widely quoted as being a problem in 2-D gel analysis and the associated sample preparation steps. This modification occurs when iso-cyanate, a urea break-down product, covalently modifies lysine residues, thus inducing a change in isoelectric point. Urea is used at up to 9 M concentrations in sample preparation and 2-D gels because of its ability to disrupt protein structure and effect denaturation without the need for ionic surfactants such as SDS. We have studied carbamylation using 7 M urea and 2 M thiourea, under a range of experimental temperatures to establish when, and if, it occurs and what can be done to minimize the modification. The actual time required for protein extraction from a tissue is usually short compared to the time required for procedures such as reduction and alkylation and IPG rehydration and focusing. Therefore, it is the temperature during these post-extraction procedures that is the most critical factor. Our experiments have shown that carbamylation does not occur during electrophoresis in the presence of urea, even with prolonged run-times. However, under poorly controlled sample preparation and storage conditions, it can become a major event. Keywords: two-dimensional electrophoresis • proteomics • carbamylation • artifacts • reduction • alkylation • MALDI-TOF mass spectrometry" @default.
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• W2023387648 date "2003-03-01" @default.
• W2023387648 modified "2023-10-17" @default.
• W2023387648 title "Carbamylation of Proteins in 2-D ElectrophoresisMyth or Reality?" @default.
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• W2023387648 doi "https://doi.org/10.1021/pr025564b" @default.
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