Abstract
To further elucidate and understand bovine milk protein composition and its relation to bioactivity, we have investigated the bovine whey proteome by gel-based proteomic methods, after first fractionating whey from late-lactation milk into acidic, basic and non-bound fractions by semi-coupled anion and cation exchange chromatography. Characteristic two-dimensional gel fingerprints were obtained for each fraction, with protein isoform patterns clearly apparent. A large number of minor whey proteins were identified, several of which have not been reported previously in bovine milk. Notably, a cluster of osteopontin peptides not priorly described in milk was consistently observed in the acidic protein fraction, presupposing novel bioactivities.
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