Skip to main content
SpringerLink
Log in

Chemical and enzymological characterization of an indonesian variant of human erythrocyte carbonic anhydrase II, CAIIJogjakarta (17 Lys → Glu)

  • Published:
Biochemical Genetics Aims and scope Submit manuscript

Abstract

A new variant of human erythrocyte carbonic anhydrase II (CAII) was discovered in a single heterozygous individual during routine screening of blood samples from the island of Java in Indonesia. The normal and variant components of the heterozygous CAII mixture were resolved by isoelectric focusing following purification by a specific affinity matrix. Specific esterase activities and Michaelis-Menten constants were identical. Only very small differences were noted with respect to inhibition by acetazolamide and chloride. Double diffusion analysis showed the immunological identity of the normal and variant enzymes. The variant CAII was considerably less heat stable than the normal enzyme. The variant was slightly more stable than the normal enzyme upon dialysis against the zinc chelator dipicolinic acid (PDCA), indicating a tighter binding of zinc than the normal enzyme. Analysis of tryptic peptides from the normal and variant enzymes indicated that, in the variant, lysine at position 17 from the N terminus had changed to glutamic acid. The differences in physiochemical properties observed for the normal and variant enzyme are discussed in relation to the possible effects of this substitution on the structure of the CAII molecule.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Anderson, B., Nyman, P. D., and Strid, L. (1972). Amino acid sequence of human erythrocyte carbonic anhydrase B. Biochem. Biophys. Res. Commun. 48670.

    Google Scholar 

  • Blake, N. M. (1978). Genetic variants of carbonic anhydrase in the Asian-Pacific area. Ann. Hum. Biol. 5557.

    Google Scholar 

  • Carter, N. D. (1972). Carbonic anhydrase isozymes in Cavia porcellus, Cavia aperea and their hybrids. Comp. Biochem. Physiol. 43B743.

    Google Scholar 

  • Carter, N. D., Shiels, A., and Tashian, R. E. (1978). Carbonic anhydrase III isoenzyme from human and bovine muscle. Biochem. Soc. Trans. 6552.

    Google Scholar 

  • De Simone, J., Linde, M., and Tashian, R. E. (1973). Evidence for linkage of carbonic anhydrase isoezyme genes in the pig-tailed macaque. Nature New Biol. 24255.

    Google Scholar 

  • Eicher, E. M., Stern, R. H., Womack, J. E., Davisson, M. T., Roderick, T. H., and Reynolds, S. C. (1976). Evolution of mammalian carbonic anhydrase loci by tandem duplication: Close linkage of Car 1 and Car 2 to the centromere region of chromosome 3 of the mouse. Biochem. Genet. 14651.

    Google Scholar 

  • Funakoshi, S., and Deutsch, H. F. (1969). Human carbonic anhydrases II—some physico-chemical properties of native isozymes and of similar isozymes generated in vitro. J. Biol. Chem. 2443438.

    Google Scholar 

  • Hall, G. E., and Schraer, R. (1979). Purification and partial characterization of high and low activity carbonic anhydrase isoenzymes from Malaclemys Terrapin Centrata. Comp. Biochem. Physiol. 63561.

    Google Scholar 

  • Henderson, L. E., Henriksson, D., and Nyman, P. O. (1976). Primary structure of human carbonic anhydrase C. J. Biol. Chem. 2515457.

    Google Scholar 

  • Hopkinson, D. A., Coppock, J. S., Muhlemann, M. F., and Edwards, Y. H. (1974). The detection and differentiation of the products of the human carbonic anhydrase loci, CAI and CAII using fluorogenic substrates. Ann. Hum. Genet. 38155.

    Google Scholar 

  • Houmard, J., and Drapeau, G. R. (1972). Staphylococcal protease: A proteolytic enzyme specific for glutamoyl bonds. Proc. Natl. Acad. Sci. USA 693506.

    Google Scholar 

  • Jones, G. L., and Shaw, D. C. (1982). A polymorphic variant of human erythrocyte carbonic anhydrase I with a widespread distribution in Australian Aborigines, CAIAustralia-9 (8 Asp → Gly): Purification, properties, amino acid substitution, and possible physiological significance of the variant enzyme. Biochem. Genet. 20943.

    Google Scholar 

  • Laemmli, U. K. (1970). Cleavage and structural proteins during the assembly of the head of bacteriophage T4. Nature 227680.

    Google Scholar 

  • Liljas, A., Kannan, K. K., Bugsten, P. C., Waara, I., Fridborg, K., Strondberg, U., Carlbom, L., Järup, S., Lövgren, S., and Petef, M. (1972). Crystal structure of human carbonic anhydrase C. Nature New Biol. 234131.

    Google Scholar 

  • Lin, K. T. D., and Deutsch, H. F. (1972). Human carbonic anhydrases. VIII. Isolation and characterization of a polymorphic form of a C type isozyme. J. Biol. Chem. 2473761.

    Google Scholar 

  • Lin, K. T. D., and Deutsch, H. F. (1973). Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B. J. Biol. Chem. 2481885.

    Google Scholar 

  • Lin, K. T. D., and Deutsch, H. F. (1974). Human carbonic anhydrases. XII. The complete primary structure of carbonic anhydrase C. J. Biol. Chem. 2492329.

    Google Scholar 

  • Linkdskog, S., Henderson, L. E., Kannan, K. K., Liljas, A., Nyman, P. O., and Strandberg, B. (1971). Carbonic anhydrase. In Boyer, P. D. (ed.), The Enzymes, Vol. 5 Academic Press, New York and London, p. 602.

    Google Scholar 

  • Notstrand, B., Vaara, I., and Kannan, K. K. (1975). Structural relationship of human erythrocyte carbonic anhydrase isozymes B and C. In Markert, C. L. (ed.), Isozymes, Vol. 1 Academic Press, New York, pp. 575–599.

    Google Scholar 

  • Osborne, W. R. A., and Tashian, R. E. (1974). Thermal inactivation studies of normal and variant human erythrocyte carbonic anhydrase by using a sulphonamide binding assay. Biochem. J. 141219.

    Google Scholar 

  • Osborne, W. R. A., and Tashian, R. E. (1975). An improved method for the purification of carbonic anhydrase isozymes by affinity chromatography. Anal. Biochem. 64297.

    Google Scholar 

  • Ouchterlony, O. (1953). Antigen-antibody reactions in gels. IV. Types of reaction in co-ordinated systems of diffusion. Acta Pathol. Microbiol. Scand. 22231.

    Google Scholar 

  • Righetti, P. G., and Drysdale, J. W. (1976). Isoelectric focussing. In Work, J. S., and Work, E. (eds.), Laboratory Techniques in Biochemistry and Molecular Biology, Vol. 5 North-Holland, Amsterdam and Oxford, pp. 388–390.

    Google Scholar 

  • Tashian, R. E. (1977). Evolution and regulation of the carbonic anhydrase isozymes. In Rattazi, M. C., Scandalois, J. C., and Whitt, G. S. (eds.), Isozymes: Current Topics in Biological and Medical Research, Vol. 2 Alan R. Liss, New York, pp. 21–62.

    Google Scholar 

  • Tashian, R. E., Hewett-Emmett, D., and Goodman, M. (1980a). Evolutionary diversity in the structure and activity of carbonic anhydrase. Protides Biol. Fluids 28153.

    Google Scholar 

  • Tashian, R. E., Kendall, A. G., and Carter, N. D. (1980b). Inherited variants of human red cell carbonic anhydrases. Hemoglobin 4635.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Human Biology, John Curtin School of Medical Research, Australian National University, Canberra, Australia

    Graham L. Jones & A. Salam M. Sofro

  2. Department of Physical Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra, Australia

    Denis C. Shaw

Authors
  1. Graham L. Jones
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. A. Salam M. Sofro
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Denis C. Shaw
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Jones, G.L., Sofro, A.S.M. & Shaw, D.C. Chemical and enzymological characterization of an indonesian variant of human erythrocyte carbonic anhydrase II, CAIIJogjakarta (17 Lys → Glu). Biochem Genet 20, 979–1000 (1982). https://doi.org/10.1007/BF00484072

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00484072

Key words

Search

Navigation