Genetic polymorphism of an α1‐ protease inhibitor in mink plasma

Abstract

Two‐dimensional electrophoretic analysis of mink (Mustela vison Schreber) plasma proteins was done by a first‐dimension separation in agarose gel (pH 8.6), followed by a second dimension in horizontal polyacrylamide gel (pH 9.0). Two α1‐globulins, designated Pi‐1 and Pi‐2, and another protein, designated Pi‐3 were found to inhibit the esterolytic activity of bovine trypsin and bovine chymotrypsin. The Pi‐1 segregation analysis in limited family data supported the hypothesis that the three Pi‐1 types observed were controlled by two codominant, autosomal alleles. Each of the Pi‐1 homozygote types showed one strong, broad fraction while the Pi‐1 heterozygote type had two fractions. The electrophoretic mobility and patterns of Pi‐1 indicated that this protein was most probably identical to the polymorphic post albumin (Pa) in mink plasma, reported by Saison in 1968. © 1981 Mendelian Society of Lund