The complete amino acid sequence of bovine antithrombin (ATIII)

Journal of Protein Chemistry - Tập 10 - Trang 205-212 - 1991
H. Mejdoub1,2, M. Le Ret1, Y. Boulanger1, M. Maman3, J. Choay3, J. Reinbolt1
1Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique, Strasbourg Cedex, France
2ENIS, Sfax, Tunisia
3Sanofi Recherche-Centre Choay, Gentilly Cedex, France

Tóm tắt

Bovine antithrombin (ATIII) is a glycoprotein of Mr 56,600. Its primary structure was established using peptide sequences from five different digests. Bovine ATIII exhibits four glycosylation sites as well as human ATIII. The primary structures of bovine and human ATIII were compared: all the residues required for the integrity of the heparin-binding domain are strictly conserved. However, there are differences in the secondary structures of both proteins, bovine and human ATIII.

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Björk, I., Danielsson, A., Fenton, J. W., and Jörnvall, H. (1981).FEBS Lett. 126, 257–260. Blackburn, M. N., Smith, R. L., Carson, J., and Sibley, C. C. (1984).J. Biol. Chem. 259, 939–941. Brennan, S. O., George, P. M., and Jordan, R. E. (1987).FEBS Lett. 219, 431–436. Carrell, R. W., Jeppson, J. O., Laurell, C. B., Brennan, S. O., Owen, M. C., Vaughan, L., and Boswell, D. R. (1982).Nature 298, 329–333. Chandra, T., Stackhouse, R., Kidd, V. J., and Woo, S. L. C. (1983).Proc. Natl. Acad. Sci. 80, 1845–1848. Chang, J. Y. (1989).J. Biol. Chem. 264, 3111–3115. Chang, J. Y., and Tran, T. H. (1986).J. Biol. Chem. 261, 1174–1176. Choay, J., Petitou, M., Lormeau, J. C., Sinaÿ, P., Casu, B., and Gatti, G. (1983).Biochem. Biophys. Res. Commun. 116, 492–499. Chou, P. Y., and Fasman, G. D. (1978).Advances in Enzymology 47, 45–147. Delarue, M., Samama, J. P., Mourey, L., and Moras, D. (1990).Acta Cryst. B46, 550–556. Devereux, J., Haeberli, P., and Smithies, O. (1984).Nucl. Acids Res. 12, 387–395. Drapeau, G. R. (1980).J. Biol. Chem. 255, 839–840. Fontana, A. (1972).Methods in Enzymology 25, 419–423. Franzen, L. E., Svensson, S., and Larm, O. (1980).J. Biol. Chem. 255, 5090–5093. Garnier, J., Osguthorpe, D. J., and Robson, B. (1978).J. Mol. Biol. 120, 97–120. Gribskov, M., Burgess, R. R., and Devereux, J. (1986).Nucl. Acids Res. 14, 327–334. Gross, E., and Witkop, B. (1962).J. Biol. Chem. 237, 1856–1860. Hewick, R. M., Hunkapiller, M. W., Hood, L. E., and Dreyer, W. J. (1981).J. Biol. Chem. 256, 7990–7997. Houmard, J., and Drapeau, R. (1972).Proc. Natl. Acad. Sci. 69, 3506–3509. Huber, R., and Carrell, R. W. (1989).Biochemistry 28, 8951–8966. Jordon, R. E., Oosta, G. M., Gardner, W. T., and Rosenberg, R. D. (1980).J. Biol. Chem. 255, 10,081–10,090. Jörnvall, H., Fish, W. W., and Björk, I. (1979).FEBS Lett. 106, 358–362. Koide, T., Odani, S., Takahashi, K., Ono, J., and Sakuragawa, N. (1984).Proc. Natl. Acad. Sci. 81, 289–293. Kurachi, K., Schmer, G., Hermodson, M. A., Teller, D. C., and Davie, E. W. (1976).Biochemistry 15, 368–372. Kyte, J., and Doolittle, R. F. (1982).J. Mol. Biol. 157, 105–132. Liu, C. S., and Chang, J. Y. (1987).J. Biol. Chem. 262, 17,356–17,361. Metz-Boutigue, M. H., Jolles, J., Jolles, P., Mazurier, J., Spik, G., and Montreuil, J. (1980).Biochim. Biophys. Acta 622, 308–314. Nordenman, B., Nyström, C., and Björk, I. (1977).Eur. J. Biochem. 78, 195–203. Okazaki, K., Yamada, H., and Imoto, T. (1985).Anal. Biochem.,149, 516–520. Owen, M. C., Brennan, S. O., Lewis, J. H., and Carrell, R. W. (1983).N. Engl. J. Med. 309, 694. Peterson, C. B., Noges, C. M., Pecon, J. M., Church, F. C., and Blackburn, M. N. (1987).J. Biol. Chem. 262, 8061–8065. Rosenberg, R. D. (1977).Fed. Proc. Fed. Amer. Soc. Exp. Biol. 36, 10–18. Samama, J. P., Delarue, M., Mourey, L., Choay, J., and Moras, D. (1989).J. Mol. Biol. 210, 877–879. Sun, X. J., and Chang, J. Y. (1989).J. Biol. Chem. 264, 11,288–11,293. Thaler, E., and Schmer, G. (1975).Br. J. Haematol. 31, 233–243. Travis, J., and Salvensen, J. S. (1983).Annu. Rev. Biochem. 52, 655–709.