Polymorphic serum prealbumin (Pa) of pig, identified as an a!‐protease inhibitor

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Abstract
Summary: Pig serum proteins were analysed by horizontal polyacrylamide gel electrophoresis, with a discontinuous buffer system (pH 9.0). A 12 % acrylamide concentration in the separation gel was used. Each of the two prealbumin (Pa) alleles gave rise to two closely migrating fractions. The polymorhic Pa was identified as an a,‐protease inhibitor as the Pa fractions inhibited the esterolytic activity of both bovine trypsin and chymotrypsin. Therefore, it has been proposed that the locus symbol for this prealbumin be changed to Pi‐1. The protease inhibitory spectra and electrophoretic mobility of the Pa (Pi‐1) fractions suggested that this protein was probably the same as the pig serum a,‐protease inhibitor described in some earlier studies and that it corresponds to human serum a,‐protease inhibitor (Pi).