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.
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