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Two‐dimensional gel electrophoresis of cattle plasma proteins: Genetic polymorphism of an α1‐protease inhibitor
Author(s) -
Juneja R. K.,
Gahne B.
Publication year - 1980
Publication title -
animal blood groups and biochemical genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.756
H-Index - 81
eISSN - 1365-2052
pISSN - 0003-3480
DOI - 10.1111/j.1365-2052.1980.tb01512.x
Subject(s) - biology , trypsin , allele , polymorphism (computer science) , pi , agarose , microbiology and biotechnology , trypsin inhibitor , gel electrophoresis , blood proteins , polyacrylamide gel electrophoresis , allele frequency , chymotrypsin , transferrin , globulin , albumin , genetics , enzyme , biochemistry , gene , endocrinology
Summary Two‐dimensional electrophoretic analysis of cattle plasma proteins was done by a first dimension separation in agarose gel (pH 5.0), followed by a second dimension in horizontal polyacrylamide gel (pH 9.0). This method resulted in improved and reproducible separation of many α‐ and β‐globulins. Three groups of a‐globulins, designated Pi‐1, Pi‐2 and Pi‐3, were found to inhibit the estero‐lytic activity of bovine trypsin and bovine chymotrypsin. Pi‐2 showed appreciable inhibition only for trypsin and genetic polymorphism was observed for this protein. Family data supported the hypothesis that the three Pi‐2 types observed were controlled by two codominant, autosomal alleles. The occurrence of a third Pi‐2 allele was also postulated in some animals studied. The frequency of the most common allele, Pi‐2 s , ranged from 0.5‐0.8 in the different breeds of cattle studied (Swedish Red and White, Friesian, Jersey, Charolais and Simmental). The post‐transferrins Ptf‐1 and Ptf‐2 in cattle plasma were shown to be two different genetic systems.