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.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Andersson, B., Nyman, P.-O., and Strid, L. (1972). Amino acid sequence and human erythrocyte carbonic anhydrase B. Biochem. Biophys. Res. Commun. 48670.
Bray, R. P. (1977). Primary Structural Studies of Horse Carbonic Anhydrases Doctoral dissertation, University of Wisconsin, Madison.
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.
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.
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.
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.
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.
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.
Furth, A. J. (1968). Purification and properties of horse erythrocyte carbonic anhydrases. J. Biol. Chem. 2434832.
Giraud, N., Marriq, C., and Laurent-Tabusse, G. (1974). Structure primarie de l'anhydrase carbonique erythrocytaire B humaine. Biochimie 561031.
Henderson, L. E., Henriksson, D., and Nyman, P. O. (1976). Primary structure of human carbonic anhydrase C. J. Biol. Chem. 2515457.
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.
Jabusch, J. R., and Deutsch, H. F. (1981). The sequence of the high activity equine erythrocyte carbonic anhydrase. Fed. Proc. 40794.
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.
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.
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.
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.
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.
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.
Tanis, R. J., Ferrell, R. E., and Tashian, R. E. (1974). Amino acid sequence of sheep carbonic anhydrase C. Biochim. Biophys. Acta 371534.
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.
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.
Author information
Authors and Affiliations
Additional information
This investigation was supported in part by United States Public Health Service Grant CA-1786 from the National Cancer Institute.
Rights and permissions
About this article
Cite this article
Jabusch, J.R., Deutsch, H.F. Sequence of the high-activity equine erythrocyte carbonic anhydrase: N-terminal polymorphism (acetyl-ser/acetyl-thr) and homologies to similar mammalian isozymes. Biochem Genet 22, 357–367 (1984). https://doi.org/10.1007/BF00484234
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00484234