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Egg albumen polymorphisms in the Fowl: loci II and III

Published online by Cambridge University Press:  14 April 2009

I. E. Lush
I. E. Lush
Affiliation:
Agricultural Research Council Poultry Research Centre, Edinburgh, 9
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The genetics of two polymorphic loci in the fowl was studied. Each affects the electrophoretic mobility of a different egg albumen protein, and at each locus two alleles were shown to segregate in a Mendelian manner.

The polymorphic proteins are not any of the well-characterized egg albumen proteins, viz. ovalbumin, ovomucoid, ovomucin, flavoprotein, avidin and lysozyme.

In contrast to all others, two hens were found to have an anomalous, variable, phenotype. A tentative explanation of this was offered.

Type
Research Article
Information
Genetics Research , Volume 5 , Issue 1 , February 1964 , pp. 39 - 49
Copyright
Copyright © Cambridge University Press 1964

References

REFERENCES

Baker, C. M. A. & Manwell, C. (1962). Molecular genetics ofavian proteins I. The egg white proteins of the domestic fowl. Brit. Poult. Sci. 3, 161–174.CrossRefGoogle Scholar
Brooks, J. & Hale, H. P. (1961). The mechanical properties of the thick white of the hen's egg. II. The relation between rigidity and composition. Biochim. biophys. Acta, 46, 289–301.CrossRefGoogle Scholar
Cochrane, D. & Annau, E. (1962). Electrophoretic differences in the egg-white proteins of the hen. Canad. J. Biochem. & Physiol. 40, 1335–1341.CrossRefGoogle ScholarPubMed
Cole, A. G. (1932). Preparation of crystallised egg albumin (ovalbumin). Proc. Soc. exp. Biol., N.Y., 30, 1162–1164.CrossRefGoogle Scholar
Flynn, F. & de Mayo, P. (1951). Microeleetrophoresis of protein on filter paper. Lancet, 2, 235.CrossRefGoogle ScholarPubMed
Forsythe, R. H. & Foster, J. F. (1950). Egg white proteins I. Electrophoretic studies on whole white. J. biol. Chem. 184, 377–383.CrossRefGoogle ScholarPubMed
Frampton, V. L. & Romanoff, A. L. (1947). Some physiochemical properties of the three albumin layers of the chicken, goose and emu egg. Arch. Biochem. 13, 315–321.Google Scholar
Fredericq, E. & Deutsch, H. F. (1949). Studies on ovomucoid. J. biol. Chem. 181, 499.CrossRefGoogle ScholarPubMed
Hughes, T. R. & Kiotz, I. M. (1956). Metal-Protein Complexes. In Advances in Biochemical Analysis, 3.CrossRefGoogle ScholarPubMed
Ingram, V. M. (1961). Haemoglobin and its abnormalities. Springfield: C. C. Thomas.Google Scholar
Lowe, V. P. W. & McDougall, E. I. (1961). Serum β-globulin types in red deer and other species and their stability in the presence of bacteria. Nature, Lond., 192, 983–984.CrossRefGoogle Scholar
Lush, I. E. (1961). Genetic polymorphisms in the egg albumen proteins of the domestic fowl. Nature, Lond., 189, 981–984.CrossRefGoogle ScholarPubMed
Mandeles, S. (1960). Use of DEAE -cellulose in the separation of proteins from egg white and other biological materials. J. Chromatog. 3, 256–264.CrossRefGoogle Scholar
McIndoe, W. M. (1962). The occurrence of two plasma albumins in the domestic fowl. Nature, Lond., 195, 353–354.CrossRefGoogle Scholar
Ogden, A. L., Morton, J. R., Gilmour, D. G. & McDermid, E. M. (1962). Inherited variants in the transferrins and conalbumins of the chicken. Nature, Lond., 195, 1026–1028.CrossRefGoogle ScholarPubMed
Poulik, M. (1957). Starch gel electrophoresis in a discontinuous system of buffers. Nature, Lond., 180, 1477–1479.CrossRefGoogle Scholar
Poulik, M. & Smithies, O. (1958). Comparison and combination of the starch gel and filter paper electrophoretic methods: two-dimensional electrophoresis. Biochem. J. 68, 636–643.CrossRefGoogle ScholarPubMed
Perlmann, G. E. (1949). The electrophoretic properties of plakalbumin. J. Amer. chem. Soc. 71, 1146.CrossRefGoogle ScholarPubMed
Rhodes, M. B., Azari, P. R. & Feeney, R. E. (1958). Analysis, fractionation, and purification of egg white proteins with cellulose-cation exchanger. J. biol. Chem. 230, 399–408.CrossRefGoogle ScholarPubMed
Rhodes, M. B., Bennett, N. & Feeney, R. E. (1959). The Flavoprotein-Apoprotein system of egg white. J. biol. Chem. 234, 2054–2060.CrossRefGoogle ScholarPubMed
Romanoff, A. L. & Sullivan, R. A. (1937). Refractive index of egg albumen: changes with age, season and development. Ind. Eng. Chem. 29, 117–120.CrossRefGoogle Scholar
Romanoff, A. L. & Romanoff, A. J. (1949). The Avian Egg. New York: John Wiley & Sons, Inc.Google Scholar
Smithies, O. (1955). Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults. Biochem. J. 61, 629–641.CrossRefGoogle ScholarPubMed
Warner, R. C. & Weber, I. (1951). The preparation of crystalline conalbumin. J. biol. Chem. 191, 173–180.CrossRefGoogle ScholarPubMed
Williams, J. (1962). A comparison of conalbumin and transferrin in the domestic fowl. Biochem. J. 83, 355–364.CrossRefGoogle ScholarPubMed