Abstract
Two-dimensional electrophoretic analysis of water-soluble proteins of chicken egg yolk was done by a first-dimension separation in agarose gel (pH 8.6) followed by a second-dimension separation in horizontal polyacrylamide gel (pH 9.0). Genetic polymorphism of a protein, tentatively designated as Pr M prealbumin, was observed. The analysis of family data suggests that the Pr M prealbumin is controlled by two alleles, Pr M+ and Pr M-, at a single autosomal locus. The Pr M+ allele appears to be dominant to the Pr M- allele.
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