Advertisement

Biochemical Genetics

, Volume 22, Issue 3–4, pp 357–367 | Cite as

Sequence of the high-activity equine erythrocyte carbonic anhydrase: N-terminal polymorphism (acetyl-ser/acetyl-thr) and homologies to similar mammalian isozymes

  • Jack R. Jabusch
  • Harold F. Deutsch
Article

Abstract

The amino acid sequence of the high-activity equine erythrocyte carbonic anhydrase (CA-II) has been determined. Two different N-termini are noted, the C1 form having an N-acetyl-serine and the C2 form an N-acetyl-threonine. The sequence of the equine enzyme is most homologous to the human CA-II isozyme, with 224 of the 259 residues being identical.

Key words

equine carbonic anhydrase enzyme polymorphism 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Andersson, B., Nyman, P.-O., and Strid, L. (1972). Amino acid sequence and human erythrocyte carbonic anhydrase B. Biochem. Biophys. Res. Commun. 48670.Google Scholar
  2. Bray, R. P. (1977). Primary Structural Studies of Horse Carbonic Anhydrases Doctoral dissertation, University of Wisconsin, Madison.Google Scholar
  3. Contel, E. P. B., Hewett-Emmett, D., Stroup, S. K., and Tashian, R. E. (1981). Amino acid sequence of chimpanzee carbonic anhydrase I (CA I): Evolutionary implications for the origin of human and great apes. Isozyme Bull. 1444.Google Scholar
  4. Curtis, P. J., Withers, E., Demuth, D., Watt, R., Venta, P. J., and Tashian, R. E. (1983). The Nucleotide sequence and derived amino acid sequence of cDNA coding for mouse carbonic anhydrase II. Gene 25325.Google Scholar
  5. Deutsch, H. F., and Bray, R. P. (1975). Carbonic anhydrase isozymes in American ponies and riding horses. A new polymorphic high activity type isozyme. Biochem. Genet. 13643.Google Scholar
  6. Deutsch, H. F., Fundkoshi, S., Fujita, T., Taniguchi, N., and Hirai, H. (1972). Isolation in crystalline form and properties of six horse erythrocyte carbonic anhydrases. J. Biol. Chem. 2474499.Google Scholar
  7. Deutsch, H. F., Jabusch, J. R., and Lin, K.-T. D. (1977). Purification and properties of a polymorphic high activity equine erythrocyte carbonic anhydrase. J. Biol. Chem. 252555.Google Scholar
  8. Ferrell, R. E., Stroup, S. K., Tanis, R. J., and Tashian, R. E. (1978). Amino acid sequence of rabbit carbonic anhydrase II. Biochim. Biophys. Acta 5331.Google Scholar
  9. Furth, A. J. (1968). Purification and properties of horse erythrocyte carbonic anhydrases. J. Biol. Chem. 2434832.Google Scholar
  10. Giraud, N., Marriq, C., and Laurent-Tabusse, G. (1974). Structure primarie de l'anhydrase carbonique erythrocytaire B humaine. Biochimie 561031.Google Scholar
  11. Henderson, L. E., Henriksson, D., and Nyman, P. O. (1976). Primary structure of human carbonic anhydrase C. J. Biol. Chem. 2515457.Google Scholar
  12. Henriksson, D., Tanis, R. J., and Tashian, R. E. (1980). The amino acid sequence of carbonic anhydrase I from the rhesus macaque. Biochem. Biophys. Res. Commun. 96135.Google Scholar
  13. Jabusch, J. R., and Deutsch, H. F. (1981). The sequence of the high activity equine erythrocyte carbonic anhydrase. Fed. Proc. 40794.Google Scholar
  14. Jabusch, J. R., Bray, R. P., and Deutsch, H. F. (1980). Sequence of the low activity equine erythrocyte carbonic anhydrase and delineation of the amino acid substitutions in various polymorphic forms. J. Biol. Chem. 2559196.Google Scholar
  15. 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
  16. Lin, K.-T. D., and Deutsch, H. F. (1974). Human carbonic anhydrases. XII. The complete primary structure of the C isozyme. J. Biol. Chem. 2492329.Google Scholar
  17. Notstrand, B., Waare, I., and Kannan, K. K. (1974). Structural relationship of human crythrocyte carbonic anhydrase isozymes B and C. In Markert, C. L. (Ed.), Isozymes, Vol I Academic Press, New York, p. 575.Google Scholar
  18. Sciaky, M., Limozin, N., Fillippi-Fovean, D., Guilian, J. M., and Laurent-Tabusse, G. (1976). Primary structure of bovine erythrocyte carbonic anhydrase CI. I. Complete amino acid sequence. Biochimie 581071.Google Scholar
  19. Smithies, O., Gibson, D., Fanning, E. M., Goodfleisch, R. M., Gilman, J. G., and Ballantyne, D. L. (1971). Quantitative procedures for use with the Edman-Begg sequenator. Partial sequences of two unusual immunoglobulin light chains, Rzf and Sac. Biochemistry 104912.Google Scholar
  20. Tanis, R. J., Ferrell, R. E., and Tashian, R. E. (1974). Amino acid sequence of sheep carbonic anhydrase C. Biochim. Biophys. Acta 371534.Google Scholar
  21. Tashian, R. E., Hewett-Emmett, D., Stroup, S. K., Goodman, M., and Yu, Y.-S. L. (1980). Evolution of structure and function in the carbonic anhydrase isozymes of mammals. In Bauer, C., Gross, G., and Bartels, H. (eds.), Biophysics and Physiology of Carbon Dioxide, p. 165.Google Scholar
  22. Tashian, R. E., Hewett-Emmett, D., and Goodman, M. (1983). On the evolution and genetics of carbonic anhydrase I, II and III. In Isozymes: Current Topics in Biological and Medical Research. Vol. 7: Molecular Structure and Regulation Alan R. Liss, New York, pp. 79–100.Google Scholar

Copyright information

© Plenum Publishing Corporation 1984

Authors and Affiliations

  • Jack R. Jabusch
    • 1
  • Harold F. Deutsch
    • 1
  1. 1.Department of Physiological ChemistryUniversity of Wisconsin—MadisonMadison

Personalised recommendations