Journal
ELECTROPHORESIS
Volume 31, Issue 17, Pages 2903-2912Publisher
WILEY
DOI: 10.1002/elps.200900764
Keywords
2-DE; Glycoprotein; Sialic acid
Funding
- Ministerio de Educacion y Ciencia [BIO 2004-0438, BIO 2007-61323]
- Foundation La Marato de TV3 [050932]
- Government of Catalonia [2005SGR00065]
- National Institute for Bioprocessing Research and Training, Ireland
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2-DE is broadly used for quantitative analysis of differential protein expression in complex mixtures such as serum samples or cell lysates. PTMs directly influence the 2-DE pattern, and knowledge of the rules of protein separation is required in order to understand the protein distribution in a 2-DE gel. Glycosylation is the most common PTM and can modify both the molecular weight and the pI of a protein. In particular, the effect of charged monosaccharides (mainly sialic acids, SAs) on the 2-DE pattern of a protein is of major interest since changes in sialylation are regularly observed in comparative studies. Little is known about the pI shift of a glycoprotein induced by the presence of SAs, or whether this shift is the same for all glycoproteins. To address this issue, this study examined the influence of SA on the 2-DE pattern of three serum glycoproteins (haptoglobin, alpha 1-antitrypsin and ribonuclease 1), which N-glycan chains had been previously characterised, and reviewed existing bibliographic data. The SA content of the different glycoforms of a glycoprotein showed a negative linear correlation with the pI, although the slope varied among the studied glycoproteins. We also described a positive correlation between the protein pI and the pI decrease per SA molecule.
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