Abstract
Genetic control of the level of blood catalase activity was first demonstrated in 1927. At present, such control has been demonstrated or suggested for nine different species, including man, the most studied. The development of an acatalasemic strain of mice has permitted a wide variety of experimental approaches, including most of those used in humans. Among those approaches which cannot readily be applied to man but have been used in acatalasemic mice are investigations of sensitivity to radiation lethality, mechanism of awareness to radiation, possible use as a model for replacement therapy for inborn errors of metabolism, and catalase in tissues other than erythrocytes. These are described, together with genetic, immunological, and other studies comparable to similar work on acatalasemic humans.
Similar content being viewed by others
References
Aebi, H., Heiniger, J. P., Bütler, R., and Hässig, A. (1961). Two cases of acatalasia in Switzerland. Experientia 17 466.
Aebi, H., Heiniger, J. P., and Lauber, E. (1964). Methämoglobinbildung in Erythrocyten durch Peroxideinwirkung. Versuche zur Beurteilung der Schutzfunktion von Katalase und Glutathionperoxidase. Helv. Chim. Acta 47 1428.
Aebi, H., Suter, H., and Feinstein, R. N. (1968). Activity and stability of catalase in blood and tissues of normal and acatalasemic mice. Biochem. Genet. 2 245.
Allison, A. C., ap Rees, W., and Burn, G. P. (1957). Genetically controlled differences in catalase activity of dog erythrocytes. Nature 180 649.
Baur, E. W. (1963). Catalase abnormality in a Caucasian family in the United States. Science 140 816.
Campbell, D. H., and Fourt, L. (1939). Immunochemistry of catalase. J. Biol. Chem. 129 385.
Cohen, G., and Hochstein, P. (1963). Glutathione peroxidase: The primary agent for the elimination of hydrogen peroxide in erythrocytes. Biochemistry 2 1420.
Dickerman, R. C., Feinstein, R. N., and Grahn, D. (1968). Position of the acatalasemia gene in linkage group V of the mouse. J. Heredity 59 177.
Feinstein, R. N. (1949). Perborate as substrate in a new assay of catalase. J. Biol. Chem. 180 1197.
Feinstein, R. N., Berliner, S., and Green, F. O. (1958). Mechanism of inhibition of catalase by 3-amino-1,2,4-triazole. Arch. Biochem. Biophys. 76 32.
Feinstein, R. N., Howard, J. B., Ballonoff, L. B., and Seaholm, J. E. (1964a). A rapid blood catalase screening technique adjustable to any level of activity. Anal. Biochem. 8 277.
Feinstein, R. N., Seaholm, J. E., Howard, J. B., and Russell, W. L. (1964b). Acatalasemic mice. Proc. Natl. Acad. Sci. 52 661.
Feinstein, R. N., Howard, J. B., Braun, J. T., and Seaholm, J. E. (1966a). Acatalasemic and hypocatalasemic mouse mutants. Genetics 53 923.
Feinstein, R. N., Braun, J. T., and Howard, J. B. (1966b). Reversal of H2O2 toxicity in the acatalasemic mouse by catalase administration. Suggested model for possible replacement therapy of inborn errors of metabolism. J. Lab. Clin. Med. 68 952.
Feinstein, R. N., Braun, J. T., and Howard, J. B. (1967a). Acatalasemic and hypocatalasemic mouse mutants. II. Mutational variations in blood and solid tissue catalases. Arch. Biochem. Biophys. 120 165.
Feinstein, R. N., Sacher, G. A., Howard, J. B., and Braun, J. T. (1967b). Comparative heat stability of blood catalase. Arch. Biochem. Biophys. 122 338.
Feinstein, R. N., Suter, H., and Jaroslow, B. N. (1968a). Blood catalase polymorphism: Some immunological aspects. Science 159 638.
Feinstein, R. N., Braun, J. T., and Howard, J. B. (1968b). Nature of the heterozygote blood catalase in a hypocatalasemic mouse mutant. Biochem. Genet. 1 277.
Feinstein, R. N., Faulhaber, J. T., and Howard, J. B. (1968c). Acatalasemia and hypocatalasemia in the dog and the duck. Proc. Soc. Exptl. Biol. Med. 127 1051.
Feinstein, R. N., Faulhaber, J. T., and Howard, J. B. (1968d). Sensitivity of acatalasemic mice to acute and chronic irradiation and related conditions. Radiation Res. 35 341.
Holman, R. A. (1956). Production of abnormal bacteria. Some possible analogies with formation of tumours. Lancet 271 515.
Kol'tsov, N. K. (1927). The catalase content in the blood of vertebrates as a genetic trait. Zh. Eksperim. Biol. Med. 5 303.
Kultjugin, A. (1926). Über die Abnahme der Katalasewirkung des Blutes beim Aufbewahren. Biochem. Z. 167 241.
Micheli, A., Peetoom, F., Rose, N., Ruddy, S., and Grabar, P. (1960). Immunochemical study of hemolyzates of human red blood cells. III. Identification of erythrocyte catalase. Ann. Inst. Pasteur 98 694.
Morris, D. D., and Feinstein, R. N. (1969). Mechanism of mouse awareness of X-radiation. Nature 222 688.
Putilin, K. I. (1929). Quoted in Allison et al. (1957).
Radev, T. (1960). Inheritance of hypocatalasemia in guinea pigs. J. Genet. 57 169.
Richardson, M., Huddleson, I. F., Bethea, R., and Trustdorf, M. (1953). Study of catalase in erythrocytes and bacteria. II. Catalase activity of erythrocytes from different species of normal animals and from normal humans. Arch. Biochem. Biophys. 42 124.
Scandalios, J. G. (1965). Subunit dissociation and recombination of catalase isozymes. Proc. Natl. Acad. Sci. 53 1035.
Shaw, C. R. (1964). The use of genetic variation in the analysis of isozyme structure. Brookhaven Symp. Biol. 17 117.
Szeinberg, A., de Vries, A., Pinkhas, J., Djaldetti, M., and Ezra, R. (1963). A dual hereditary red blood cell defect in one family; hypocatalasemia and glucose-6-phosphate dehydrogenase deficiency. Acta Geneticae Medicae et Gemellologiae 12 247.
Takahara, S. (1952). Progressive oral gangrene probably due to lack of catalase in the blood (acatalasemia). Lancet 263 1101.
Tanford, C., and Lovrien, R. (1962). Dissociation of catalase into subunits. J. Am. Chem. Soc. 84 1892.
Tria, E. (1939). Anticatalase. J. Biol. Chem. 129 377.
von Wartburg, J. P., Papenberg, J., and Aebi, H. (1965). An atypical human alcohol dehydrogenase. Can. J. Biochem. 43 889.
Warburg, O., Gawehn, K., and Geissler, A. W. (1957). Über die Wirkung von Wasserstoffperoxyd auf Krebszellen und auf embryonale Zellen. Z. Naturforsch. 12b 393.
Author information
Authors and Affiliations
Additional information
This paper was presented at a symposium entitled “Genetic Control of Mammalian Metabolism” held at The Jackson Laboratory, Bar Harbor, Maine, June 30–July 2, 1969. The symposium was supported in part by an allocation from NIH General Research Support Grant FR 05545 from the Division of Research Resources to The Jackson Laboratory.
Work supported by the United States Atomic Energy Commission.
Rights and permissions
About this article
Cite this article
Feinstein, R.N. Acatalasemia in the mouse and other species. Biochem Genet 4, 135–155 (1970). https://doi.org/10.1007/BF00484026
Issue Date:
DOI: https://doi.org/10.1007/BF00484026