Proteomic characterization by 2-DE in bovine serum and whey from healthy and mastitis affected farm animals.

Acute phase proteins (APP) have been identified in whey and sera from healthy and mastitis cows through the proteomic analysis using two-dimensional electrophoresis (2-DE) coupled with Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry (MALDI-TOF MS). Although normal and mastitis serum samples show relatively similar protein composition, marked differences in expression levels and patterns can be observed. Conversely, normal and mastitis whey showed a very different composition, likely due to extravasation of blood proteins to the mammary gland. Different isoforms from the most abundant protein in milk, casein, were detected in both normal and mastitis whey. Other proteins, such as lactotransferrin, were only detected in the inflamed animal samples. Immunoglobulins showed different patterns but not increased levels in the inflamed whey. Also, many cellular proteins in mastitis cow's whey, that were absent from healthy cow's milk. They are responsible for the great change in composition between normal and mastitis whey, especially those which exert a biological function related to immune defense. Data collected in this work are of interest for gaining information about physiological changes in protein patterns in different fluids and, the correspondent modifications as result of an acute phase process in farm. This article is part of a Special Issue entitled: Proteomics: The clinical link.
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