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Zur Natur und ontogenetischen Entwicklung von Carboanhydrase-Isoenzymen in menschlichen Erythrozyten

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Zusammenfassung

Im menschlichen Erythrozyten finden sich 2 genetisch determinierte Carboanhydrasen, CA I und CA II. Mit besonderen Techniken lassen sich weitere Isoenzyme nachweisen. Diese wurden jetzt erstmals bei Kindern verschiedener Reifegrade und Altersstufen und bei Schilddrüsenerkrankungen untersucht. Es zeigte sich, daß die Minorfraktionen in 2 Gruppen zerfallen, von denen die eine in engem Zusammenhang mit CA I, die andere mit CA II steht. Durch alkalische Inkubation konnten die Minorfraktionen direkt aus CA I bzw. CA II generiert werden. In jungen Erythrozyten war der Anteil der Minorfraktionen geringer als in alten.

In den Erythrozyten Frühgeborener ist die Carboanhydraseaktivität bis zur 32. Schwangerschaftswoche stark vermindert; sie nimmt dann bis zum Ende des ersten Lebensjahres rasch zu, erreicht die Erwachsenenwerte aber erst im Kleinkindesalter. Dabei geht die Synthese des CA II-Systems der des CA I-Systems voraus. Diese Entwicklung verläuft protrahierter als die Ablösungsvorgänge der Hämoglobinontogenese. Bei Hyperthyreose wird das gesamte CA I-System unterdrückt.

Summary

There are two different, genetically determined carboanhydrases, CA I and CA II, in human erythrocytes. With special techniques even more isoenzymes can be demonstrated. These minor fractions were investigated in premature babies, in children of different ages, and in patients with thyroid disease. It was demonstrated that the minor isoenzyme fractions were coherent with either CA I or CA II. The minor fractions could be generated from CA I or CA II by alkaline incubation. Reticulocytes contained less minor fractions than old erythrocytes.

Until the 32nd week of gestation erythrocyte carboanhydrase activity is low, increasing rapidly until the end of the first year of life, but reaching the adult level only after a few years. The synthesis of the CA II-system precedes that of the CA I-system. These developmental changes occur more slowly than those of hemoglobin ontogenesis. In hyperthyroidism the CA I-system is suppressed.

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Literatur

  1. Armstrong, J. McD., D. V. Myers, J. A. Verpoorte and J. T. Edsall: Purification and properties of human erythrocyte carbonic anhydrases. J. biol. Chem.241, 5137 (1966).

    Google Scholar 

  2. Berfenstam, R.: Studies on carbonic anhydrase in children. Acta paed.41, 32 (1952).

    Google Scholar 

  3. Betke, K.: Der menschliche Blutfarbstoff bei Fetus und reifem Organismus. Springer-Verlag, Berlin-Göttingen-Heidelberg 1954.

    Google Scholar 

  4. Betke, K., H. R. Marti and I. Schlicht: Estimation of small percentages of fetal hemoglobin. Nature184, 187 (1959).

    Google Scholar 

  5. Derrien, Y. and G. Laurent: Les anhydrases carboniques érythrocytaires. Expos. Ann. Biochim. Méd.29, 167 (1969).

    Google Scholar 

  6. Edsall, J. T.: Multiple molecular forms of carbonic anhydrase in erythrocytes. Ann. N. Y. Acad. Sci.151, 41 (1968).

    Google Scholar 

  7. Funakoshi, S. and H. F. Deutsch: Human carbonic anhydrases. I. Isolation and demonstration of isozymes in erythrocytes. J. biol. Chem.243, 6474 (1968).

    Google Scholar 

  8. Funakoshi, S. and H. F. Deutsch: Human carbonic anhydrases. II. Some physicochemical properties of native isozymes and of similar isozymes generated in vitro. J. biol. Chem.244, 3438 (1969).

    Google Scholar 

  9. Funakoshi, S. and H. F. Deutsch: Human carbonic anhydrases. III. Immunochemical studies. J. biol. Chem.245, 2852 (1970).

    Google Scholar 

  10. Garby, L. and M. Hjelm: Ultracentrifugal fractionation of human erythrocytes with respect to cell age. Blut9, 284 (1963).

    Google Scholar 

  11. Gibbons, B. H. and J. T. Edsall: Kinetic studies of human carbonic anhydrases B and C. J. biol. Chem.239, 2539 (1964).

    Google Scholar 

  12. Gitlin, D., T. Sasaki and P. Vuopio: Immunochemical quantitation of proteins in single cells. I. Carbon anhydrase B, β-chain hemoglobin and γ-chain hemoglobin in some normal and abnormal erythrocytes. Blood32, 796 (1968).

    Google Scholar 

  13. Graham, J. L. and B. W. Grunbaum: A rapid method for microelectrophoresis and quantitation of hemoglobins on cellulose acetate. Amer. J. clin. Path.39, 567 (1963).

    Google Scholar 

  14. Guest, G. M. and E. W. Brown: Erythrocytes and hemoglobin of the blood in infancy and childhood. Amer. J. Dis. Child.93, 486 (1957).

    Google Scholar 

  15. Headings, V. E. and R. E. Tashian: A radioimmunoassay for quantifying carbonic anhydrase isozymes in crude lysates. Biochem. Genet.4, 285 (1970).

    Google Scholar 

  16. Headings, V. E. and R. E. Tashian: Isoenzymes of carbonic anhydrase I from primate red blood cells. Biochim. Biophys. Acta236, 353 (1971).

    Google Scholar 

  17. Jonxis, J. H. P. and H. K. A. Visser: Determination of low percentages of foetal haemoglobin in blood of normal children. Amer. J. Dis. Child:92, 588 (1956).

    Google Scholar 

  18. Kleihauer, E., H. Braun und K. Betke: Demonstration von fetalem Hämoglobin in den Erythrozyten eines Blutausstriches. Klin. Wschr.35, 637 (1957).

    Google Scholar 

  19. Laurent, G., M. Charrel, D. Garcon, M. Castay, C. Marriq et Y. Derrien: Sur les protéines accompagnant l'hémoglobine humaine dans ses préparations. Bull. Soc. Chim. Biol.46, 603 (1964).

    Google Scholar 

  20. Laurent, G., C. Marriq, D. Nahon et Y. C. P. Herrien: Isolement des protéines «lentes» Y1, X1 et X2 accompagnants l'hémoglobine humaine dans ses préparations. Soc. Biol.156, 1456 (1962).

    Google Scholar 

  21. Magid, E.: Determination of erythrocyte carbonic anhydrase B and C: An aid in the diagnosis of thyroid disorders? Scand. J. clin. Lab. Invest.26, 257 (1970).

    Google Scholar 

  22. Maren, T. H.: A simplified micromethod for the determination of carbonic anhydrase and its inhibitors. J. Pharmacol. Exp. Ther.130, 26 (1960).

    Google Scholar 

  23. Maren, Th.: Carbonic anhydrase: Chemistry, physiology and inhibition. Physiol. Rev.47, 595 (1967).

    Google Scholar 

  24. Marti, H. R.: Normale und anormale menschliche Hämoglobine. Springer-Verlag, Berlin-Göttingen-Heidelberg 1963.

    Google Scholar 

  25. Nörgaard-Pedersen, B. and M. Mondrup: Quantitative estimation of human carbonic anhydrases B and C by electrophoresis in antibody containing agarose. Scand, J. Clin. & Lab. Invest.27, 169 (1971).

    Google Scholar 

  26. Nyman, P. O.: Purification and properties of carbonic anhydrase from human erythrocytes. Biochim. Biophys. Acta52, 1 (1961).

    Google Scholar 

  27. O'Connel, D. J., C. J. Caruso and M. D. Sass: Separation of erythrocytes of different ages. Clin. Chem.11, 771 (1965).

    Google Scholar 

  28. Poblete, E., D. W. Thibeault and P. A. M. Auld: Carbonic anhydrase in the premature. Ped.42, 429 (1968).

    Google Scholar 

  29. Raper, A. B.: The occurrence of foetal erythropoiesis after infancy. Arch. Dis. Childh.38, 353 (1963).

    Google Scholar 

  30. Rickli, E. E., S. A. S. Ghazanfar, B. H. Gibbons and J. T. Edsall: Carbonic anhydrase from human erythrocytes; preparation and properties of two enzymes. J. biol. Chem.239, 1065 (1964).

    Google Scholar 

  31. Ruiz-Reyes, G. and M. D. J. Ramirez-Zorilla: Rapid measurement of erythrocyte carbonic anhydrase isozymes by means of cellulose acetate membrane electrophoresis. Amer. J. clin. Path.50, 677 (1968).

    Google Scholar 

  32. Shows, Th. B.: The amino acid substitution and some chemical properties of a variant human erythrocyte carbonic anhydrase: Carbonic anhydrase IdMichigan. Biochem. Genet.1, 171 (1967).

    Google Scholar 

  33. Tashian, R. E.: The esterases and carbonic anhydrases of human erythrocytes. In: Yunis, J. J., Biochemical methods in red cell genetics. Academic Press. New York-London 1969.

    Google Scholar 

  34. Tashian, R. E. and M. W. Shaw: Inheritance of an erythrocyte acetylesterase variant in man. Amer. J. Hum. Genet.14, 295 (1962).

    Google Scholar 

  35. Theorell, H.: 8th. Intern. Congress of Biochem. 1970, Abstract p. 75.

  36. Weatherall, D. J. and J. P. McIntyre: Development and acquired variations in erythrocyte carbonic anhydrase isozymes. Brit. J. Haemat.13, 106 (1967).

    Google Scholar 

  37. Wehinger, H.: Rapid demonstration of minor carboanhydrase isoenzyme fractions in human erythrocytes. Klin. Wschr.50, 339 (1972).

    Google Scholar 

  38. Wehinger, H.: Untersuchungen über die Erythrozyten-Carboanhydrasen bei pathologischen Zuständen im Kindesalter. Z. f. Kinderheilk., im Druck.

  39. Wehinger, H. and M. Alebouyeh: Densitometrisch-quantitative Bestimmung von Hämoglobin A2 nach Mikrozonen-Elektrophorese auf Cellulose-Acetat-Folie. Klin. Wschr.48, 701 (1970).

    Google Scholar 

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  1. Helmut Wehinger

    Present address: Universitäts-Kinderklinik Freiburg i. Brsg., Mathildenstraße 1, D-78, Freiburg i. Brsg.

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    Wehinger, H. Zur Natur und ontogenetischen Entwicklung von Carboanhydrase-Isoenzymen in menschlichen Erythrozyten. Blut 27, 172–185 (1973). https://doi.org/10.1007/BF01634032

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    • DOI: https://doi.org/10.1007/BF01634032

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