Summary
The amino acid sequence of lysozyme c from chachalaca egg white was determined. Like other bird lysozymes c, that of the chachalaca has 129 amino acid residues. It differs from other avian lysozymes c by 27 to 31 amino acid substitutions as well as by being devoid of phenylalanine. It contains substitutions at 9 positions which are invariant in the other 7 bird lysozymes of known sequence. Although the chachalaca is classified zoologically in the order Galliformes, which includes chickens and other pheasant-like birds, its lysozyme differs more from those of pheasant-like birds than do the lysozymes c of ducks. Phylogenetic analysis of the sequence comparisons confirms that the lineage leading to chachalaca lysozyme c separated from that leading to other galliform lysozymes c before the duck lysozyme c lineage did. This indicates a contrast between protein evolution and evolution at the organismal level. Immunological comparison of chachalacalysozyme c with other lysozymes of known sequence provides further support for the proposal that immunological cross-reactivity is strongly dependent on degree of sequence resemblance among bird lysozymes.
Similar content being viewed by others
References
Arnon, R., Sela, M. (1969). Proc.Natl.Acad.Sci.USA 62, 163
Atassi, M.Z. (1975). Immunochemistry 12, 423
Braunitzer, G., Schrank, B., Ruhfus, A. (1970). Z.Physiol.Chem. 351, 1589
Browne, W.J., North, A.C.T., Phillips, D.C., Brew, K., Vanaman, T.C., Hill, R.L. (1969). J.Mol.Biol. 42, 65
Canfield, R.E. (1963). J.Biol.Chem. 238, 2698
Canfield, R.E., Kammerman, S., Sobel, J.H., Morgan, F.J. (1971). Nature New Biol. 232, 16
Champion, A.B., Prager, E.M., Wachter, D., Wilson, A.C. (1974). Microcomplement fixation. In: Biochemical and immunological taxonomy of animals, C.A. Wright, ed., p. 397. London: Academic Press
Champion, A.B., Soderberg, K.L., Wilson, A.C., Ambler, R.P. (1975). J.Mol.Evol. 5, 291
Dalgliesh, C.E. (1952). Biochem.J. 52, 3
Doolittle, R.F., Blombäck, B. (1964). Nature 202, 147
Edman, P., Begg, G. (1967). Eur.J.Biochem. 1, 80
Fainaru, M., Wilson, A.C., Arnon, R. (1974). J.Mol.Biol. 84, 635
Farris, J.S. (1972). Am.Natur. 106, 645
Fitch, W.M., Margoliash, E. (1967). Science 155, 279
Fujio, H., Imanishi, M., Nishioka, K., Amano, T. (1968). Biken J. 11, 207
Fujio, H., Martin, R.E., Ha, Y.-M., Sakato, N., Amano, T. (1974). Biken J. 17, 73
Fujio, H., Sakato, N., Amano, T. (1971). Biken J. 14, 395
Hermann, J., Jollès, J. (1970). Biochim.Biophys.Acta 200, 178
Hermann, J., Jollès, J., Buss, D.H., Jollès, P. (1973). J.Mol.Biol. 79, 587
Hermann, J., Jollès, J., Jollès, P. (1971). Eur.J.Biochem. 24, 12
Hill, R.L., Steinman, H.M., Brew, K. (1974). Comparison of the structures of alpha-lactalbumin and lysozyme. In: Lysozyme, E.F. Osserman, R.E. Canfield, S. Beychok, eds., p. 55. New York: Academic Press
Hudson, G.E., Parker, R.A., Vanden Berge, J., Lanzillotti, P.J. (1966). Amer.Midl.Nat. 76, 1
Jollès, J., Jauregui-Adell, J., Bernier, I., Jollès, P. (1963). Biochim. Biophys.Acta 78, 668
Jollès, J., Jollès, P. (1969). Helv.Chim.Acta 52, 2671
Jollès, J., Jollès, P. (1971). Helv.Chim.Acta 54, 2668
Jollès, J., Jollès, P. (1972). Fed.Eur.Biochem.Soc.Lett. 22, 31
Jollès, J., Van Leemputten, E., Mouton, A., Jollès, P. (1972). Biochim. Biophys.Acta 257, 497
Kaneda, M., Kato, I., Tominaga, N., Titani, K., Narita, K. (1969). J.Biochem.(Tokyo) 66, 747
King, M.-C., Wilson, A.C. (1975). Science 188, 107
Laemmli, U.K. (1970). Nature 227, 680
LaRue, J.N., Speck, J.C., Jr. (1970). J.Biol.Chem. 245, 1985
Lee, B., Richards, F.M. (1971). J.Mol.Biol. 55, 379
Neville, D.M., Jr. (1971). J.Biol.Chem. 246, 6328
Prager, E.M., Arnheim, N., Mross, G.A., Wilson, A.C. (1972). J.Biol.Chem. 247, 2905
Prager, E.M., Brush, A.H., Nolan, R.A., Nakanishi, M., Wilson, A.C. (1974a). J.Mol.Evol. 3, 243
Prager, E.M., Fainaru, M., Wilson, A.C., Arnon, R. (1974b). Immunochemistry 11, 153
Prager, E.M., Wilson, A.C., Arnheim, N. (1974c). J.Biol.Chem. 249, 7295
Prager, E.M., Wilson, A.C. (1971a). J.Biol.Chem. 246, 523
Prager, E.M., Wilson, A.C. (1971b). J.Biol.Chem. 246, 5978
Prager, E.M., Wilson, A.C. (1971c). J.Biol.Chem. 246, 7010
Prager, E.M., Wilson, A.C. (1972). Biochem.Genet. 7, 269
Prager, E.M., Wilson, A.C. (1975). Proc.Natl.Acad.Sci.USA 72, 200
Sharon, N., Eshdat, Y., Maoz, I., Bernstein, Y., Prager, E.M., Wilson, A.C. (1974). Israel J.Chem. 12, 591
Spies, J.R., Chambers, D.C. (1949). Anal.Chem. 21, 1249
Swank, R.T., Munkres, K.D. (1971). Anal.Biochem. 39, 462
Thomsen, J., Lund, E.H., Kristiansen, K., Brunfeldt, K., Malmquist, J. (1972). Fed.Eur.Biochem.Soc.Lett. 22, 34
Tung, J.-S., Knight, C.A. (1972). Anal.Biochem. 48, 153
Waugh, A.E. (1943). Elements of statistical methods. New York and London: McGraw-Hill Book Co., Inc.
Whetmore, A. (1960). Smithson.Misc.Collect. 139, 1
Wilson, A.C., Maxson, L.R., Sarich, V.M. (1974a). Proc.Natl.Acad.Sci.USA 71, 2843
Wilson, A.C., Prager, E.M. (1974). Antigenic comparison of animal lysozymes. In: Lysozyme, E.F. Osserman, R.E. Canfield, S. Beychok, eds., p. 127. New York: Academic Press
Wilson, A.C., Sarich, V.M., Maxson, L.R. (1974b). Proc.Natl.Acad.Sci.USA 71, 3028
Author information
Authors and Affiliations
Additional information
103rd communication on lysozymes from the Laboratory of P. Jollès. Supported in part by grants from C.N.R.S. (ER 102), I.N.S.E.R.M. (Groupe de recherche U-116), N.S.F. (GB-42028X), and N.I.H. (GM-21509).
Rights and permissions
About this article
Cite this article
Jollés, J., Schoentgen, F., Jollès, P. et al. Amino acid sequence and immunological properties of chachalaca egg white lysozyme. J Mol Evol 8, 59–78 (1976). https://doi.org/10.1007/BF01738883
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF01738883