Abstract
The blood catalase of a hypocatalasemic mouse mutant has been compared with that of the wild-type (normal) animal and with that of the heterozygote. Comparison is on the basis of stability to heat and to urea. Electrophoretic evidence is of no value, because all forms tested show the same mobility. Because the heterozygote heat and urea inactivation curves differ from those of the two parental forms, and because the curves are smoothly S-shaped, with no shoulders or other irregularities, it is suggested that this heterozygote produces only a single molecular form of the enzyme.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
(1964) Brookhaven Symp. Biol. 17.
(1963) Cold Spring Harbor Symp. Quant. Biol. 28.
(1964) Cold Spring Harbor Symp. Quant. Biol. 29.
Feinstein, R. N. (1949). J. Biol. Chem. 180 1197.
Feinstein, R. N., Howard, J. B., Braun, J. T., and Seaholm, J. E. (1966). Genetics 53 923.
Feinstein, R. N., Braun, J. T., and Howard, J. B. (1967). Arch. Biochem. Biophys. 120 165.
Feinstein, R. N., Sacher, G. A., Howard, J. B., and Braun, J. T. (1967). Arch. Biochem. Biophys. (in press).
Micheli, A., Peetoom, F., Rose, N., Ruddy, S., and Grabar, P. (1960). Ann. Inst. Pasteur 98 694.
Riley, V. (1960). Proc. Soc. Exptl. Biol. Med. 104 751.
Shaw, C. R. (1964). Brookhaven Symp. Biol. 17 117.
Author information
Authors and Affiliations
Additional information
Work supported under the auspices of the U.S. Atomic Energy Commission.
Rights and permissions
About this article
Cite this article
Feinstein, R.N., Braun, J.T. & Howard, J.B. Nature of the heterozygote blood catalase in a hypocatalasemic mouse mutant. Biochem Genet 1, 277–285 (1968). https://doi.org/10.1007/BF00485182
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00485182