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ABSTRACT: Background
Tissue factor (TF) is a single polypeptide integral membrane glycoprotein composed of 263 residues and is essential to life in its role as the initiator of blood coagulation. Previously we have shown that the activity of the natural placental TF (pTF) and the recombinant TF (rTF) from Sf9 insect cells is different (Krudysz-Amblo, J. et al (2010) J. Biol. Chem. 285, 3371-3382).Methods
In this study, using mass spectrometry, we show by quantitative analysis that the extent of glycosylation varies on each protein.Results and conclusions
Fractional abundance of each glycan composition at each of the three glycosylation sites reveals the most pronounced difference to be at asparagine (Asn) 11. This residue is located in the region of extensive TF-factor VIIa (
SUBMITTER: Krudysz-Amblo J
PROVIDER: S-EPMC3048926 | biostudies-literature | 2011 Apr
REPOSITORIES: biostudies-literature