Hostname: page-component-7f64f4797f-bnl7t Total loading time: 0 Render date: 2025-11-04T05:03:54.657Z Has data issue: false hasContentIssue false
  • English
  • Français

A serum esterase variation in Microtus agrestis (L.)

Published online by Cambridge University Press:  14 April 2009

M. A. Russell  and
R. Semeonoff
M. A. Russell
Affiliation:
Institute of Animal Genetics, Edinburgh
R. Semeonoff
Affiliation:
Institute of Animal Genetics, 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. An investigation of the serum esterases of the field-vole, M. agrestis, has been carried out by the method of starch-gel electrophoresis.

2. A total of 254 animals, mainly from Carron Valley, near Stirling, have been examined.

3. Evidence is presented for a system of four enzymes controlled by two genetic loci, which it is proposed to call Es-3C and Es-3R.

4. Each locus specifies one polypeptide sub-unit of the E3 enzyme, which is a dimer.

5. The two loci each have two alleles present at high frequencies in the population examined.

Information

Type
Research Article
Information
Genetics Research , Volume 10 , Issue 2 , October 1967 , pp. 135 - 142
Copyright
Copyright © Cambridge University Press 1967

References

REFERENCES

Augustinsson, K. B. (1959). Electrophoresis studies on blood plasma esterases. Acta chem. scand. 13, 571.CrossRefGoogle Scholar
Hunter, R. L. & Markert, C. L. (1957). Histochemical demonstration of enzymes separated by zone electrophoresis in starch gels. Science, N.Y. 125, 1294.Google Scholar
Kaplan, N. O. (1965). Lactic dehydrogenase—structure and function. Brookhaven Symp. Biol. 17, 131.Google Scholar
Lewontin, R. C. & Hubby, J. L. (1966). A molecular approach to the study of genetic heterozygosity in natural populations. II. Genetics, 54, 595.CrossRefGoogle Scholar
Lewontin, R. C. & White, M. J. D. (1960). Interaction between inversion polymorphism of two chromosome pairs in Moraba scurra. Evolution, Lancaster, Pa. 14, 116.Google Scholar
Markert, C. L. & Möller, F. (1959). Multiple forms of enzymes: tissue, ontogenetic and species specific patterns. Proc. natn. Acad. Sci. U.S.A. 45, 753.CrossRefGoogle ScholarPubMed
Poulik, M. D. (1957). Starch gel electrophoresis in a discontinuous system of buffers. Nature, Lond., 180, 1477.CrossRefGoogle Scholar
Semeonoff, R. & Robertson, F. W. (in preparation).Google Scholar
Shaw, C. R. (1965). The use of genetic variation in the analysis of isozyme structure. Brook-haven Symp. Biol. 17, 117.Google Scholar
Smith, K. D., Ursprung, H. & Wright, T. R. F. (1963). Xanthine dehydrogenase in Drosophila: detection of isozymes. Science, N.Y. 142, 226.CrossRefGoogle ScholarPubMed
Smithies, O. (1955). Zone electrophoresis in starch gel. Biochem. J. 61, 629.CrossRefGoogle Scholar