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A variation in mouse kidney pyruvate kinase activity determined by a mutant gene on chromosome 9

Published online by Cambridge University Press:  14 April 2009

F. M. Johnson ,
Fred Chasalow ,
Gretchen Anderson ,
Paul Macdougal ,
R. Wayne Hendren  and
Susan E. Lewis
F. M. Johnson
Affiliation:
Laboratory of Biochemical Genetics, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina 27709
Fred Chasalow
Affiliation:
Chemistry and Life Sciences Group, Research Triangle Institute, Research Triangle Park, North Carolina 27709
Gretchen Anderson
Affiliation:
Chemistry and Life Sciences Group, Research Triangle Institute, Research Triangle Park, North Carolina 27709
Paul Macdougal
Affiliation:
Chemistry and Life Sciences Group, Research Triangle Institute, Research Triangle Park, North Carolina 27709
R. Wayne Hendren
Affiliation:
Chemistry and Life Sciences Group, Research Triangle Institute, Research Triangle Park, North Carolina 27709
Susan E. Lewis
Affiliation:
Chemistry and Life Sciences Group, Research Triangle Institute, Research Triangle Park, North Carolina 27709
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Summary

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Pyruvate kinase activity was studied in kidney extracts of mice from various sources. One C57BL/6J female among several hundred examined expressed activity approximately one half of the normal level. This animal transmitted the trait, and a single gene responsible for the activity difference was identified and mapped to chromosome 9. Linkage with Mod-1 and dilute was established. A spontaneous mutation in the C57BL/6J strain apparently was responsible for the variant pyruvate kinase.

Type
Research Article
Information
Genetics Research , Volume 37 , Issue 2 , April 1981 , pp. 123 - 131
Copyright
Copyright © Cambridge University Press 1981

References

REFERENCES

Burtis, C. H., Johnson, W. F., Mailen, J. C., Overton, J. B., Tiffany, T. O. & Watsky, J. B. (1973). Development of an analytical system based around a miniature fast analyzer. Clinical Chemistry 19, 895–903.CrossRefGoogle ScholarPubMed
Burtis, C. A., Johnson, W. F. & Overton, J. B. (1974). Automated loading of discrete, microliter volumes of lipids into a miniature fast analyzer. Analytical Chemistry 46, 786–789.CrossRefGoogle Scholar
Burtis, C. A., Mailen, J. C., Johnson, W. F., Scott, C. D., Tiffany, T. O. & Anderson, N. G. (1972). Development of a miniature fast analyzer. Clinical Chemistry 18, 753–761.CrossRefGoogle ScholarPubMed
Cardenas, J. M. & Dyson, R. D. (1978). Mammalian pyruvate kinase hybrid isozymes: tissue distribution and physiological significance. Journal of Experimental Zoology 204, 361–368.CrossRefGoogle ScholarPubMed
Johnson, F. M. (1979). Germinal mutations in the mouse resolved by electrophoresis and centrifugal fast analyzer. Genetics 91, s55.Google Scholar
Johnson, F. M., Chasalow, F., Lewis, S. E., Barnett, L. & Lee, C.-Y. (1980 a). A null allele at the Mod-1 locus of the house mouse. Journal of Heredity (submitted).Google Scholar
Johnson, F. M., Chasalow, F., Roberts, G. T., Sharma, R. K., Zweidinger, R., Morgan, A. & Lewis, S. E. (1980 b). The detection of mutants in mice by electrophoresis: results of a model induction experiment with procarbazine. Genetics (submitted).Google Scholar
Johnson, F. M., Hendren, R. W., Chasalow, F., Barnett, L. B. & Lewis, S. E. (1980 c). A null mutation at the mouse phosphoglucomutase-1 locus and new locus, Pgm-3. Biochemical Genetics (submitted).Google Scholar
Lalley, P. A., Francke, U. & Minna, J. D. (1978). Conservation of autosomal gene synteny groups in mouse and man. Nature (Lond.) 274, 160–163.CrossRefGoogle ScholarPubMed
Tiffany, T. O., Chilcote, D. D. & Burtis, C. A. (1973). Evaluation of kinetic parameters by use of a small computer interfaced ‘fast analyzer’ – an addition to automated clinical enzymology. Clinical Chemistry 19, 908–918.CrossRefGoogle ScholarPubMed
Tiffany, T. O., Jansen, J. M., Burtis, C. A., Overton, J. B. & Scott, C. D. (1972). Enzymatic kinetic rate and end-point analyses of substrate, by use of a GeMSAEC fast analyzer. Clinical Chemistry 18, 829–840.CrossRefGoogle ScholarPubMed