Hostname: page-component-586b7cd67f-l7hp2 Total loading time: 0 Render date: 2024-11-28T00:02:15.479Z Has data issue: false hasContentIssue false

Genetics of plasma transferrins in the mouse

Published online by Cambridge University Press:  14 April 2009

B. L. Cohen
Affiliation:
Institute of Animal Genetics, University of Edinburgh
Rights & Permissions [Opens in a new window]

Extract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

1. The plasma proteins of six inbred strains of mice have been studied, using starch-gel electrophoresis.

2. The existence of two alternative plasma transferrin (β-globulin) phenotypes has been demonstrated. Five of the strains have one of these and one strain has the other. Each of the two transferrin patterns comprises three (or possibly only two) electrophoretic bands. The two patterns differ in all of these bands.

3. The two transferrin types recognized are determined by a pair of allelic, autosomal genes (designated TrfA and TrfB). The TrfA phenotype (CBA strain) is determined by the genotype TrfA/TrfA, and the TrfB phenotype (A, C57BL, JU, KL, RIII strains) by the genotype TrfB/TrfB. The phenotype TrfAB, of the heterozygote (genotype TrfA/TrfB), is distinguishable and shows four (or possibly only three) bands. In this way it closely resembles a mixture of equal parts of TrfA and TrfB plasma.

4. No linkage was detected between the Trf locus and sex, the agouti locus or the haemoglobin locus.

5. The possible molecular basis of the action of the transferrin alleles in the mouse, and the widespread distribution in mammals of polymorphism involving the transferrins, are discussed.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1960

References

REFERENCES

Ashton, G. C. (1958). Further β-globulin phenotypes in sheep. Nature, Lond., 182, 11011102.CrossRefGoogle ScholarPubMed
Ashton, G. C. (1959 a). β-globulin alleles in some Zebu cattle. Nature, Lond., 184, 11351136.CrossRefGoogle ScholarPubMed
Ashton, G. C. (1959 b). β-globulin polymorphism and early foetal mortality in cattle. Nature, Lond., 183, 404405.Google Scholar
Ashton, G. C. & McDougall, E. I. (1958). β-globulin polymorphism in cattle, sheep and goats. Nature, Lond., 183, 945946.Google Scholar
Carter, T. C. & Falconer, D. S. (1951). Stocks for detecting linkage in the mouse, and the theory of their design. J. Genet. 50, 307323.CrossRefGoogle ScholarPubMed
Finney, D. J. (1949). The estimation of the frequency of recombinations. J. Genet. 49, 159176.Google Scholar
Giblett, E. R., Hickman, C. G. & Smithies, O. (1959). Serum transferrins. Nature, Lond., 183, 15891590.Google Scholar
Gluecksohn-Waelsch, S., Ranney, H. M. & Sisken, B. F. (1957). The hereditary transmission of haemoglobin differences in mice. J. clin. Invest. 36, 753756.CrossRefGoogle ScholarPubMed
Grüneberg, H. (1952). The Genetics of the Mouse, 2nd ed.The Hague: Martinus Nijhoff.Google Scholar
Harris, H., Robson, E. B. & Siniscalco, M. (1958). β-globulin variants in man. Nature, Lond., 182, 452.Google Scholar
Ingram, V. M. (1956). A specific chemical difference between the globins of normal human and sickle-cell anaemia. Nature, Lond., 178, 792794.CrossRefGoogle ScholarPubMed
Owen, J. A., Silberman, H. J. & Got, C. (1958). Detection of haemoglobin, haemoglobin-haptoglobin complexes and other substances with peroxidase activity after zone electrophoresis. Nature, Lond., 182, 1373.Google Scholar
Popp, R. A. & St. Amand, W. (1959). The mouse haemoglobin locus. Anat. Rec. 132, 489.Google Scholar
Poulik, M. (1957). Starch gel electrophoresis in a discontinuous system of buffers. Nature, Lond., 180, 14771479.Google Scholar
Poulik, M. & Smithies, O. (1958). Comparison and combination of the starch gel and filter paper electrophoretic methods: two-dimensional electrophoresis. Biochem. J. 68, 636643.Google Scholar
Report of International Committee on Standardized Nomenclature for Inbred Strains of Mice (1952). Cancer Res. 12, 602613.Google Scholar
Russell, E. S. & Gerald, P. S. (1958). Inherited electrophoretic haemoglobin patterns among 20 inbred strains of mice. Science, 128. 15691570.Google Scholar
Smithies, O. (1955). Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults. Biochem. J. 61, 629641.CrossRefGoogle ScholarPubMed
Smithies, O. (1957). Variants in human serum β-globulins. Nature, Lond., 180, 14821483.Google Scholar
Smithies, O. & Hickman, C. G. (1958). Inherited variations in the serum proteins of cattle. Genetics, 43, 374385.Google Scholar
Smithies, O. & Hiller, O. (1959). The genetic control of transferrins in humans. Biochem. J. 72, 121126.Google Scholar
Thompson, S., Foster, J. F., Gowen, J. W. & Tauber, O. (1954). Hereditary differences in the serum proteins of normal mice. Proc. Soc. exp. Biol., N.Y., 87, 315317.Google Scholar