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Egg albumen polymorphisms in the fowl: The ovalbumin locus

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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1. Ovalbumin was shown, by starch gel electrophoresis, to exist in two genetically different forms, A and B. It was suggested that these are determined by two alleles at one locus, named Ov.

2. Ovalbumin of each genetic type is electrophoretically heterogeneous. Dephos-phorylation of each type with human prostatic phosphatase and calf intestinal phosphatase removed some of the heterogeneity, but some remained.

3. The genetic difference was shown not to reside in the fragment released from ovalbumin by the proteolytic enzyme subtilisin.

4. The genetic difference was evident in the ovalbumin present in the fluid contained in right oviduct cysts.

Type
Research Article
Information
Genetics Research , Volume 5 , Issue 2 , July 1964 , pp. 257 - 268
Copyright
Copyright © Cambridge University Press 1964

References

REFERENCES

Baker, C. M. A. & Manwell, C. (1962). Molecular genetics of avian proteins 1. The egg white proteins of the domestic fowl. Brit. Poult. Sci. 3, 161–174.CrossRefGoogle Scholar
Bell, D. J. (1960). Tissue components of the domestic fowl. 4. Plasma-alkaline-phosphatase activity. Biochem. J. 75, 224–229.CrossRefGoogle ScholarPubMed
Bell, D. J. & Siller, W. G. (1962). Cage layer fatigue in Brown Leghorns. Res. vet. Sci. 3, 219–230.CrossRefGoogle Scholar
Cann, J. R. (1949). Electrophoretic analysis of ovalbumin. J. Amer. chem. Soc. 71, 907–909.CrossRefGoogle ScholarPubMed
Cole, A. G. (1932). Preparation of crystallised egg albumin (ovalbumin). Proc. Soc. exp. Biol. N.Y. 30, 1162–1164.CrossRefGoogle Scholar
Cunningham, L. W., Clouse, R. W. & Ford, J. D. (1963). Heterogeneity of the carbohydrate moiety of crystalline ovalbumin. Biochim. biophys. Acta, 78, 379–381.CrossRefGoogle ScholarPubMed
Feeney, R. E., Abplanalp, H., Clary, J. J., Edwards, D. L. & Clark, J. R. (1963). A genetically varying minor protein constituent of chicken egg white. J. biol. Chem. 238, 1732–1736.CrossRefGoogle ScholarPubMed
Flavin, M. (1954). The linkage of phosphate to protein in pepsin and ovalbumin. J. biol. Chem. 210, 771–784.CrossRefGoogle ScholarPubMed
Fletcher, A. P., Marshall, R. D. & Neuberger, A. (1963). Further investigations on the carbohydrate moiety of egg albumin. Biochim. biophys. Acta, 71, 505–507.CrossRefGoogle ScholarPubMed
Guntelberg, A. V. & Ottesen, M. (1952). Preparation of crystals containing the plakal-bumin-forming enzyme from Bacillus subtilis. Nature, Lond., 170, 802.CrossRefGoogle ScholarPubMed
Guntelberg, A. V. & Ottesen, M. (1954). Purification of the proteolytic enzyme from Bacillus subtilis. C. R. Lab. Carlsberg. Sér chim. 29, 36–48.Google ScholarPubMed
Hughes, T. R. & Klotz, I. M. (1956). Metal-Protein Complexes in Advances in Biochemical Analysis. 3.CrossRefGoogle ScholarPubMed
Linderstrøm-Lang, K. & Ottesen, M. (1949). Formation of plakalbumin from ovalbumin. C. R. Lab. Carlsberg, Sér. chim. 26, 403–442.Google Scholar
Longsworth, L. G. (1939). A modification of the Schlieren method for use in electrophoretic analysis. J. Amer. chem. Soc. 61, 529–530.CrossRefGoogle Scholar
Longsworth, L. G., Cannan, R. K. & Mackinnes, D. A. J. (1940). An electrophoretic study of the proteins of egg white. J. Amer. chem. Soc. 62, 2580–2590.CrossRefGoogle Scholar
Lush, I. E. (1961). Genetic polymorphisms in the egg albumen proteins of the domestic fowl. Nature, Lond., 189, 981–984.CrossRefGoogle ScholarPubMed
Lush, I. E. (1964). Egg albumen polymorphisms in the fowl: Loci II and III. Genet. Res. 5, 39–49.CrossRefGoogle Scholar
MacPherson, C. F. C., Moore, D. H. & Longsworth, L. G. (1944). Changes in the electrophoretic composition of crystalline hen's egg albumin with age. J. biol. Chem. 156, 381–382.CrossRefGoogle Scholar
Marks, G. S., Marshall, R. D. & Neuberger, A. (1963). Carbohydrates in protein 6. Studies on the carbohydrate-peptide bond in hen's-egg albumin. Biochem. J. 87, 274–281.CrossRefGoogle ScholarPubMed
Matsushima, K. (1958). An undescribed trypsin inhibitor in egg white. Science, 127, 1178–1179.CrossRefGoogle ScholarPubMed
McBride, G. (1962). The inheritance of right oviduct development in the domestic hen. Proc. XII World's Poultry Congress, Sydney (section papers), 77–79.Google Scholar
Narita, K. & Ishii, J. (1962). N-terminal sequence in ovalbumin. J. Biochem. 52, 367–373.CrossRefGoogle Scholar
Ottesen, M. (1958). The transformation of ovalbumin into plakalbumin. C. R. Lab. Carlsberg. Sir. chim. 30, 211–270.Google ScholarPubMed
Ottesen, M. & Wollenberger, A. (1953). Stepwise degradation of the peptides liberated in the transformation of ovalbumin to plakalbumin. C. R. Lab. Carlsberg. Sér. chim. 28, 463–476.Google ScholarPubMed
Perlmann, G. E. (1949). The electrophoretic properties of plakalbumin. J. Amer. chem. Soc. 71, 1146–1149.CrossRefGoogle ScholarPubMed
Perlmann, G. E. (1952). Enzymatic dephosphorylation of ovalbumin and plakalbumin. J. gen. Physiol. 35, 711–726.CrossRefGoogle ScholarPubMed
Perlmann, G. E. (1953). Electrophoretic studies on enzymatically modified ovalbumin and casein. Disc. Faraday Soc. No. 13, 67–77.CrossRefGoogle Scholar
Perlmann, G. E. (1955). The nature of phosphorus linkages in phosphoproteins. Advanc. Protein Chem. 10, 1–30.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
Sanger, F. & Hocquard, E. (1962). Formation of dephospho-ovalbumin as an intermediate in the biosynthesis of ovalbumin. Biochem. biophys. Acta, 62, 606–607.CrossRefGoogle ScholarPubMed
Schmidt, G. (1955). In Methods in Enzymology, vol. 2, p. 529. Ed. by Colowiek, S. P. & Kaplan, N. O.New York: Academic Press Inc.Google Scholar