SearchPublisher and Institutes
You are here: Home :: Area NEM :: Medical science :: Human medicine
Barbara Cardinali, Gianluca Damonte, Luca Melone, Annalisa Salis, Francesca Tosetti, Mattia Rocco, Aldo Profumo
Identification of a new truncated form and deamidation products of fibrinopeptide B released by thrombin from human fibrinogen
Keywords: blood coagulation, human, fibrinogen, fibrinopeptides, chromatography, Mass spectrometry
Quantification of fibrinopeptides release is widely used to investigate fibrinogen activation, and standard chromatographic or capillary electrophoretic procedures are readily available. However, in the analyses of fibrinopeptide mixtures derived from the action of thrombin on human fibrinogen, a few unidentified peaks are usually present. The composition of these peaks was studied by reverse-phase HPLC/MS, revealing a single major anomalous peptide having a molecular mass of 1384.4. A further MS/MS analysis allowed the identification of this form, as a Nterminally truncated fibrinopeptide B (fpB) lacking the first two residues (pyroglutamic acid and glycine). This previously unidentified, relatively low-abundance form (7%) has been found consistently in our fibrinopeptides preparations, and analysis of the parent B-chain suggest that it is likely present in circulating fibrinogen. In addition, deamidated forms of all fpB species (including desArgB), resulting from the conversion of asparagine to aspartic acid, were also identified. Overall, these previously unreported forms constitute a substantial amount of fpB (up to 17% of the total), and should be taken into account for a reliable quantitative analysis of fpB release.
Thrombosis and Haemostasis, Schattauer
Print ISSN: 0340-6245
Volume: 96, 09/2006
Pages: 302 - 308