We characterized the two-dimensional electrophoretic patterns of fibrinogen chains α, β, and γ from the plasma of six animal species - Bos taurus, Canis familiaris, Equus caballus, Felis catus, Gallus domesticus and Sus scrofa. Comparing the spots resolved from serum and plasma samples, or exploiting the cross-reactivity of animal fibrinogen with an antiserum raised against the human protein could detect only some of the fibrinogen chains. Conversely, the analysis of the precipitate obtained by heating plasma for some minutes at 56°C was adequate for the recognition of all fibrinogen chains in all samples. Physicochemical properties of the homologous proteins were found to extensively vary across species, with complete separation among the mapping areas for α, β and γ chains and maximal heterogeneity among β chains.
Any use in proteomics for low-tech approaches? Detecting fibrinogen chains of different animal species in two-dimensional electrophoresis patterns / I. Miller, E. Gianazza, M. Gemeiner. - In: JOURNAL OF CHROMATOGRAPHY. B. - ISSN 1570-0232. - 878:25(2010), pp. 2314-2318. [10.1016/j.jchromb.2010.07.002]
Any use in proteomics for low-tech approaches? Detecting fibrinogen chains of different animal species in two-dimensional electrophoresis patterns
E. GianazzaSecondo
;
2010
Abstract
We characterized the two-dimensional electrophoretic patterns of fibrinogen chains α, β, and γ from the plasma of six animal species - Bos taurus, Canis familiaris, Equus caballus, Felis catus, Gallus domesticus and Sus scrofa. Comparing the spots resolved from serum and plasma samples, or exploiting the cross-reactivity of animal fibrinogen with an antiserum raised against the human protein could detect only some of the fibrinogen chains. Conversely, the analysis of the precipitate obtained by heating plasma for some minutes at 56°C was adequate for the recognition of all fibrinogen chains in all samples. Physicochemical properties of the homologous proteins were found to extensively vary across species, with complete separation among the mapping areas for α, β and γ chains and maximal heterogeneity among β chains.Pubblicazioni consigliate
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