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Pig plasma postalbumin-2 (alpha 1B-glycoprotein): isolation, partial characterization and immunological
A Stratil1, B Gahne, R K Juneja
1Department of Animal Breeding and Genetics, Swedish University of Agricultural Sciences, Uppsala.
Abstract:
1. Components of pig plasma postalbumin-2 (PO2) protein, after rivanol-ammonium sulphate fractionation of plasma, were separated from other proteins by an easy and rapid method of horizontal double-one dimensional IPG-PAGE. The protein was recovered from polyacrylamide gel by combination of electrophoresis and isoelectric focusing. 2. The mol. wt of PO2 was estimated to be 68,000, using SDS-PAGE. 3. Amino acid and carbohydrate compositions of PO2 were very similar to those of human plasma alpha 1B-glycoprotein (alpha 1B), confirming that PO2 is the porcine homologue of human alpha 1B. 4. Neuraminidase treatment resulted in a decrease of electrophoretic migration velocity of all four studied components of PO2. 5. Homologous proteins to pig PO2 (alpha 1B) were observed, not only in human plasma but also in plasma of dog, horse and rabbit, by immunoblotting.