Abstract
The unstable catalase variant found in the blood of individuals homozygous for Swiss-type acatalasemia and the enzyme species present in heterozygous carriers of this rare defect have been further characterized. The mutant enzyme isolated from acatalasemic red cells is considerably more heat labile and differs in electrophoretic mobility from the normal enzyme. Catalase preparations obtained from heterozygotes consist of an apparently uniform enzyme species, probably representing a molecular hybrid, with properties intermediate to those of the normal and the variant enzyme. However, antigenic identity of catalase from all three sources is observed. Model experiments indicate that hybrid catalase molecules can be produced by recombining normal and variant dimer subunits. Fractionation of erythrocytes according to density and age shows that most of the residual catalase activity is localized in juvenile acatalasemic cells, whereas in normal and heterozygous individuals the catalase activity level does not alter significantly during the life span of the red cells. These findings agree with the observation that there is no gene dosage in heterozygotes, their catalase activity values falling within the normal range.
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Aebi, H. (1972). Enzymdefekte als molekulare Krankheiten. In Verhandlungen der Deutschen Gesellschaft für innere Medizin, Vol. 78, Bergmann, Munich.
Aebi, H. (1974). In Bergmeyer, H. U. (ed.), Methoden der enzymatischen Analyse, 3rd ed., Vol. 1, Verlag Chemie, Weinheim, p. 713.
Aebi, H., and Cantz, M. (1966). Ueber die celluläre Verteilung der Katalase im Blut homozygoter und heretozygoter Defektträger (Akatalasie). Humangenetik 350.
Aebi, H., and Suter, H. (1969). Catalase. In Yunis, J. J. (ed.), Biochemical Methods in Red Cell Genetics, Academic Press, New York, p. 255.
Aebi, H., and Suter, H. (1971). Acatalasemia. In Advances in Human Genetics, Vol. 2, Plenum Press, New York.
Aebi, H., and Wyss, S. R. (1976). Acatalasemia. In Stanbury, J. B., Wyngaarden, J. B., and Frederickson, D. S. (eds.), The Metabolic Basis of Inherited Disease, 4th ed., McGraw-Hill, New York.
Aebi, H., Heiniger, J. P., Bütler, R., and Hässig, A. (1961). Two cases of acatalasia in Switzerland. Experientia 17466.
Aebi, H., Bossi, E., Cantz, M., Matsubara, S., and Suter, H. (1968a). Acatalasemia in Switzerland. In Beutler, E. (ed.), Hereditary Disorders of Erythrocyte Metabolism, Grune and Stratton, New York, p. 41.
Aebi, H., Suter, H., and Feinstein, R. N. (1968b). Activity and stability of normal and acatalasemic mice. Biochem. Genet. 2245.
Aebi, H., Wyss, S. R., and Scherz, B. (1974a). Heterogeneity of human erythrocyte catalase. In Markert, C. L. (ed.), Proceedings of the Third International Conference on Isozymes, Academic Press, New York.
Aebi, H., Wyss, S. W., Scherz, B., and Skavaril, F. (1974b). Heterogeneity of erythrocyte catalase. II. Isolation and characterization of normal and variant erythrocyte catalase and their subunits. Eur. J. Biochem. 48137.
Aebi, H., Scherz, B., Ben-Yoseph, Y., and Wyss, S. W. (1975). Dissociation of erythrocyte catalase into subunits and their re-association. Experientia 31397.
Ben-Yoseph, Y., and Shapira, E. (1973). Specific immunoassay for quantitative determination of human erythrocyte catalase. J. Lab. Clin. Med. 81133.
Bonnichson, R. (1955). In Methods in Enzymology, Vol. 2, Academic Press, New York, p. 781.
De Duve, C. (1974). Intracellular localization, biosynthesis and functions of rat liver catalase. In Thurman, R. G., Takashi, Y., Williamson, J. R., and Chance, B. (eds.), Alcohol and Aldehyde Metabolizing Systems, Academic Press, New York.
Gross, J., Hartwig, A., Botscharowa, L., Syllm-Rapoport, I., and Rosenthal, S. (1972). Dextran als Medium für die Dichtegradiententrennung von roten Blutzellen. Acta Biol. Med. Germ. 29765.
Harris, H. (1975). The Principles of Human Biochemical Genetics, 2nd ed., North-Holland, Amsterdam.
Hosoi, T., Suter, H., Yahara, S., and Aebi, H. (1969). Pseudomosaicism in acatalasemic red cells visualized by fluorescent antibody technique. Experientia 25313.
Kampen, E. J., and Zylstra, W. G. (1961). Standardization of hemoglobinometry. II. The hemiglobincyanide method. Clin. Chim. Acta 6538.
Löhr, G. W., and Waller, H. D. (1974). In Bergmeyer, H. U. (ed.), Methoden der enzymatischen Analyse, 3rd ed., Vol. 1, Verlag Chemie, Weinheim, p. 673.
Micheli, A., and Aebi, H. (1965). Recherche immunochimique de la catalase erythrocytaire dans l'hémolysat acatalasique. Rev. Etud. Clin. Biol. 10431.
Mörikofer-Zwez, S., Cantz, M., Kaufmann, H., von Wartburg, J. P., and Aebi, H. (1969). Heterogeneity of erythrocyte catalase: Correlations between sulfhydryl group content, chromatographic and electrophoretic properties. Eur. J. Biochem. 1149.
Ogata, M., Tomokuni, K., and Takahara, S. (1969). Catalatic activity of immature and mature red blood cells in Japanese acatalasemia: Difference between Japanese and Swiss acatalasemia. Acta Med. Okayama 23421.
Ogata, M., Tomokuni, K., Watanabe, S., Osaki, H., Sadamoto, M., and Takahara, S. (1972). Residual catalase in the blood of Japanese acatalasemia. Tohoku J. Exp. Med. 107105.
Ouchterlony, O. (1958). Diffusion-in-gel methods for immunological analysis. Progr. Allergy 51.
Sass, M. D. (1963). Catalase activity in young red cells. Nature 197503
Smithies, O. (1959). An improved procedure for starch-gel electrophoresis. Biochem. J. 71585.
Takahara, S. (1971). Acatalasemia and hypocatalasemia in the Orient. Semin. Hematol. 8(4397.
Thorup, O. A., Strole, W. B., and Leavell, B. S. (1961). A method for the localization of catalase on starch gels. J. Lab. Clin. Med. 58122.
Thorup, O. A., Carpenter, J. T., and Howard, P. (1964). Human erythrocyte catalase: Demonstration of heterogeneity and relationship to erythrocyte ageing in vivo. Brit. J. Haematol. 10542.
Wyss, S. R., and Aebi, H. (1975). Properties of leukocyte catalase in Swiss type acatalasemia: A comparative study of normals, heterozygotes and homozygotes. Enzyme 20257.
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This study is part of Project No. 3.384.74 subsidized by the Swiss National Science Foundation.
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Aebi, H., Wyss, S.R., Scherz, B. et al. Properties of erythrocyte catalase from homozygotes and heterozygotes for Swiss-type acatalasemia. Biochem Genet 14, 791–807 (1976). https://doi.org/10.1007/BF00485342
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DOI: https://doi.org/10.1007/BF00485342