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Saliva has emerged as an ideal diagnostic sample to explain various types of pathophysiology mainly because of ease in its
collection and strong correlation between local and systemic changes. In the present study we have profiled the proteome of
cow saliva and analyzed their functional significance. To profile the protein, the saliva collected from 3 healthy Sahiwal cows
(Bos indicus) on their day of AI. Protein was extracted from 3 animals. Equal amount of protein from each animal was pooled
and resolved on 12% SDS-PAGE. The complete lane was divided into 7 major pieces according to the intensity of bands, the gel
pieces were digested with trypsin and bRPLC were carried out. The compound lists of all the nLC MS-MS/MS fractions were
converted into MASCOT Generic Files (MGF) in ProteinScape software. A total of 441 proteins were obtained using Mascot
enabled IPI bovin database of proteins from 12 pooled bRPLC fractions, out of which 338 proteins were unique proteins
identified in this study for the first time. IgG, MUC19, albumin, Ovostatin2, Lactotransferrin and lactoperoxidase are the top
representatives of the list. The PANTHER based GO classification reveals that 39% proteins are involved in catalytic activity,
29% in binding, 12% in structural and 52% in metabolic processes which is true to the biological functions and role of the saliva
in cows. Out of these 441 proteins, 91 proteins were secretory in nature. Thus, these results provide a wide data set of bovine
salivary proteome that may serve as important biomarkers in different physiological contexts. The saliva undoubtedly is a very
excellent non-invasively collected sample which represents the physiological state of animals.