Hostname: page-component-586b7cd67f-rcrh6 Total loading time: 0 Render date: 2024-11-26T14:08:56.778Z Has data issue: false hasContentIssue false
  • English
  • Français

A dual hereditary red blood cell defect in one family: Hypocatalasemia and glucose-6-phosphate dehydrogenase deficiency

Published online by Cambridge University Press:  01 August 2014

À. Szeinberg ,
À. de Vries ,
J. Pinkhas ,
M. Djaldetti  and
R. Ezra
À. Szeinberg
Affiliation:
The Tel-Hashomer Institute of Human Genetics, Tel Aviv University, and the Rogoff Medical Research Institute, Department of Experimental Biology of the Tel Aviv University and the Labour Sickfund, Beilinson Hospital, Petah Tikva (Israel)
À. de Vries
Affiliation:
The Tel-Hashomer Institute of Human Genetics, Tel Aviv University, and the Rogoff Medical Research Institute, Department of Experimental Biology of the Tel Aviv University and the Labour Sickfund, Beilinson Hospital, Petah Tikva (Israel)
J. Pinkhas
Affiliation:
The Tel-Hashomer Institute of Human Genetics, Tel Aviv University, and the Rogoff Medical Research Institute, Department of Experimental Biology of the Tel Aviv University and the Labour Sickfund, Beilinson Hospital, Petah Tikva (Israel)
M. Djaldetti
Affiliation:
The Tel-Hashomer Institute of Human Genetics, Tel Aviv University, and the Rogoff Medical Research Institute, Department of Experimental Biology of the Tel Aviv University and the Labour Sickfund, Beilinson Hospital, Petah Tikva (Israel)
R. Ezra
Affiliation:
The Tel-Hashomer Institute of Human Genetics, Tel Aviv University, and the Rogoff Medical Research Institute, Department of Experimental Biology of the Tel Aviv University and the Labour Sickfund, Beilinson Hospital, Petah Tikva (Israel)

Summary

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.

A family of Iranian-Jewish origin with two hereditary enzymatic defects in the red blood cells, catalase deficiency and glucose-6-phosphate dehydrogenase deficiency, is described. The two enzymatic defects were inherited independently of each other. The findings are compatible with a transmission of the catalase deficiency by an autosomal gene of incomplete dominance, the homozygous state resulting in severe catalase deficiency and the heterozygous state in intermediate catalase deficiency.

Type
Research Article
Information
Acta geneticae medicae et gemellologiae: twin research , Volume 12 , Issue 3 , July 1963 , pp. 247 - 255
Copyright
Copyright © The International Society for Twin Studies 1963

References

Literature

Aebi, H., Heiniger, J. P., Bütler, R. and Hassig, A.: 1961. Two cases of acatalasia in Switzerland. Experientia, 17: 466.CrossRefGoogle ScholarPubMed
Anderson, E. P., Kalckar, H. M., Kurahashi, K. and Isselbacher, K.: 1957. A specific enzymatic assay for diagnosis of congenital galactosemia. I. The consumption test. J. Clin. Invest., 50: 469.Google ScholarPubMed
Beutler, E., Dern, R. J., Flanagan, C. L., and Alving, A. S.: 1955. The hemolytic effect of primaquine. VII. Biochemical studies of drug sensitive erythrocytes. J. Lab. Clin. Med., 45: 286.Google ScholarPubMed
Blumberg, A., Marti, H. R., Jeunet, F. and Aebi, H.: 1962. Katalase und Hamoglobindifferenzierung bei Fallen von Akatalasia. Schweiz. Med. Wochensch., 92: 1324.Google Scholar
Childs, B., Zinkham, W., Browne, E. A., Kimbro, E. L. and Torbert, J. V.: 1958. A genetic study of a defect in glutathione metabolism of the erythrocyte. Bull. Johns Hopkins Hosp., 102: 21.Google ScholarPubMed
Doxiadis, S. A., Fessas, Ph. and Valaes, T.: 1961. Glucose-6-phosphate dehydrogenase deficiency. A new aetiological factor of severe neonatal jaundice. Lancet, 1: 297.CrossRefGoogle ScholarPubMed
Kornberg, A. and Horrecker, B. L.: 1955. Glucose-6-phosphate dehydrogenase in Methods of Enzymology, Colowick, S. P. and Kaplan, N. O., eds. Academic Press, New York, Vol. I, p. 323.Google Scholar
Miller, H.: 1958. The relationship between catalase and hemoglobin in human blood. Bioch. J., 68: 275.CrossRefGoogle ScholarPubMed
Motulsky, A.: 1960. Personal communication.Google Scholar
Nishimura, E. T., Kobara, T. Y., Takahara, S., Hamilton, H. B. and Madden, S. C.: 1961. Immunologic evidence of catalase deficiency in human hereditary acatalasemia. Laboratory Invest., 10: 333.Google ScholarPubMed
Pinkhas, J., Djaldetti, M., Joshua, H., Resnick, H. and De Vries, A.: 1963. Sulfhemoglobinemia and acute hemolytic anemia with Heinz bodies following contact with a fungicide- zinc ethylene bisdithiocarbamate in a subject with glucose-6-phosphate dehydrogenase deficiency and hypocatalasemia. Blood, 21: 484.CrossRefGoogle Scholar
Ramot, B., Szeinberg, A., Adam, A., Sheba, Ch. and Gafni, D.: 1959. A study of subjects with erythrocyte glucoses-6--phosphate dehydrogenase deficiency: investigation of platelet enzymes. J. Clin. Invest., 38: 1659.CrossRefGoogle ScholarPubMed
Szeinberg, A., Sheba, Ch., Hirshorn, N. and Bodonyi, E.: 1957. Studies on erythrocytes in cases with past history of favism and drug induced acute hemolytic anemia. Blood, 12: 603.CrossRefGoogle Scholar
Szeinberg, A., Sheba, Ch. and Adam, A.: 1958. Selective occurrence of glutathione instability in red blood corpuscles of the various Jewish tribes. Blood, 13: 1043.CrossRefGoogle ScholarPubMed
Takahara, S.: 1952. Progressive oral gangrene probably due to lack of catalase in blood (acatalasemia), report of nine cases. Lancet, 2: 1101.CrossRefGoogle ScholarPubMed
Takahara, S., Hamilton, H. B., Neel, J. V., Kobara, T. Y., Ogura, Y. and Nishimura, E. T.: 1960. Hypocatalasemia: a new genetic carrier state. J. Clin. Invest., 39: 610.CrossRefGoogle ScholarPubMed
Tarlov, A. R. and Kellermeyer, R. W.: 1961. The hemolytic effect of primaquine. XI. Decreased catalase activity in primaquine sensitive erythrocytes. J. Lab. Clin. Med., 1961: 204.Google Scholar
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., 38: 122.Google Scholar
Von Euler, H.: 1934. Chemie der Enzyme, Teil, Spezielle Chemie der Enzyme. Vol. 2, part 3. Ed. J. F. Bergman, Munich, p. 72.Google Scholar