Proteomic analysis of whey and casein proteins in early milk from the marsupial Trichosurus vulpecula,the common brushtail possum |
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| Institution: | 1. Faculty of Veterinary and Agricultural Sciences, The University of Melbourne, Parkville, Victoria 3010, Australia;2. Melbourne Water, Docklands, Victoria 3008, Australia;3. The Walter and Eliza Hall Institute, Parkville, Victoria 3052, Australia;1. Kentucky Spinal Cord Injury Research Center, University of Louisville School of Medicine, 511 S. Floyd St., Rm. 616A, Louisville, KY 40202, USA;2. Department of Neurological Surgery, University of Louisville School of Medicine, 511 S. Floyd St., Rm. 616A, Louisville, KY 40202, USA;3. Department of Anatomical Sciences and Neurobiology, University of Louisville School of Medicine, 500 S. Preston St., Rm 916A, Louisville, KY 40202, USA;4. Department of Pharmacology and Toxicology, University of Louisville School of Medicine, 500 S. Preston St., Louisville, KY 40202, USA |
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| Abstract: | Whey and casein proteins representing the first and second halves of the early lactation phase in the common brushtail possum (Trichosurus vulpecula) have been compared by two dimensional gel electrophoresis. Nine components of whey were differentially expressed during early lactation, including proteins identified as cathepsin B, clusterin, late lactation protein, lysozyme, ganglioside M2 activator and neutrophil gelatinase-associated lipocalin. A major novel protein, termed very early lactation protein (VELP), was identified in whey. Partial amino acid sequence data obtained from VELP did not appear to match any other reported protein sequence. VELP was shown to be an acidic glycoprotein of 20–30 kDa which exists as a homodimer. In the casein fraction, κ-casein appeared to be differentially post-translationally modified during early lactation and fragments of β-casein were relatively more abundant at the earlier lactation stage. |
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