Abstract
Quantitative microcomplement fixation tests employing rabbit antisera were done to compare immunologically 13 cetacean myoglobins and 15 mammalian lysozymes c of known amino acid sequence. In both cases there was a strong correlation between immunological distance (y) and percent sequence difference (x), as had been found for several other globular proteins. For myoglobin the relationship could be described by y = 10.5x and for lysozyme by y = 8.5x. The coefficients in both of these equations are appreciably higher than the values of 5.1–6.9 reported for three other vertebrate globular proteins (bird lysozyme c, mammalian ribonuclease, and mammalian serum albumin), and they imply that rabbit antisera to mammalian myoglobins and lysozymes are more sensitive to evolutionary substitutions. A strong inverse correlation (r = -0.95) was found when the slope of the line relating y to x for these five data sets was plotted against the percent sequence difference between the rabbit's own protein and the proteins immunized with. Specifically, the cetacean myoglobins on average differ in amino acid sequence from rabbit myoglobin by less than 13% and exhibit the steepest slope (10.5), while bird lysozyme sequences differ by nearly 40% from rabbit lysozyme and exhibit the shallowest slope (5.1).
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Atassi MZ (1977) The complete antigenic structure of myoglobin: approaches and conclusions for antigenic structures of proteins. In: Atassi MZ (ed) Immunochemistry of proteins, vol 2. Plenum Press, New York, pp 77–176
Atassi MZ, Lee C-L (1978) The precise and entire antigenic structure of native lysozyme. Biochem J 171:429–434
Beintema JJ, Schüller C, Irie M, Carsana A (1988) Molecular evolution of the ribonuclease superfamily. Prog Biophys Molec Biol 51:165–192
Benjamin DC, Berzofsky JA, East IJ, Gurd FRN, Hannum C, Leach SJ, Margoliash E, Michael JG, Miller A, Prager EM, Reichlin M, Sercarz EE, Smith-Gill SJ, Todd PE, Wilson AC (1984) The antigenic structure of proteins: a reappraisal. Annu Rev Immun 2:67–101
Beverley SM, Wilson AC (1982) Molecular evolution in Drosophila and higher Diptera. I. Micro-complement fixation studies of a larval hemolymph protein. J Mol Evol 18:251–264
Champion AB, Prager EM, Wachter D, Wilson AC (1974) Microcomplement fixation. In: Wright CA (ed) Biochemical and immunological taxonomy of animals. Academic Press, London, pp 397–416
Champion AB, Soderberg KL, Wilson AC, Ambler RP (1975) Immunological comparison of azurins of known amino acid sequence. Dependence of cross-reactivity upon sequence resemblance. J Mol Evol 5:291–305
Hanke N, Prager EM, Wilson AC (1973) Quantitative immunological and electrophoretic comparison of primate lysozymes. J Biol Chem 248:2824–2828
He XM, Carter DC (1992) Atomic structure and chemistry of human serum albumin. Nature 358:209–215
Hirayama K, Akashi S, Furuya M, Fukuhara K (1990) Rapid confirmation and revision of the primary structure of bovine serum albumin by ESIMS and Frit-FAB LC/MS. Biochem Biophys Res Comm 173:639–646
Ibrahimi IM, Prager EM, White TJ, Wilson AC (1979) Amino acid sequence of California quail lysozyme. Effect of evolutionary substitutions on the antigenic structure of lysozyme. Biochemistry 18:2736–2744
Irwin DM, Wilson AC (1990) Concerted evolution of ruminant stomach lysozymes. Characterization of lysozyme cDNA clones from sheep and deer. J Biol Chem 265:4944–4952
Ito Y, Yamada H, Nakamura S, Imoto T (1990) Purification, amino acid sequence, and some properties of rabbit kidney lysozyme. J Biochem 107:236–241
Jollès J, Jolles P, Bowman BH, Prager EM, Stewart C-B, Wilson AC (1989) Episodic evolution in the stomach lysozymes of ruminants. J Mol Evol 28:528–535
Jollès J, Prager EM, Alnemri ES, Jollès P, Ibrahimi IM, Wilson AC (1990) Amino acid sequences of stomach and nonstomach lysozymes of ruminants. J Mol Evol 30:370–382
Jollès P, Schoentgen F, Jollès J, Dobson DE, Prager EM, Wilson AC (1984) Stomach lysozymes of ruminants. II. Amino acid sequence of cow lysozyme 2 and immunological comparisons with other lysozymes. J Biol Chem 259:11617–11625
Kendrew JC (1963) Myoglobin and the structure of proteins. Science 139:1259–1266
Lee B, Richards FM (1971) The interpretation of protein structures: estimation of static accessibility. J Mol Biol 55:379–400
Lenstra JA, Hofsteenge J, Beintema JJ (1977) Invariant features of the structure of pancreatic ribonuclease. A test of different predictive models. J Mol Biol 109:185–193
McLellan T (1984) Molecular charge and electrophoretic mobility in cetacean myoglobins of known sequence. Biochem Genet 22:181–200
Phillips DC (1974) Crystallographic studies of lysozyme and its interactions with inhibitors and substrates. In: Osserman EF, Canfield RE, Beychok S (eds) Lysozyme. Academic Press, New York, pp 9–30
Poljak RJ (1991) Structure of antibodies and their complexes with antigens. Molec Immunol 28:1341–1345
Prager EM, Brush AH, Nolan RA, Nakanishi M, Wilson AC (1974) Slow evolution of transferrin and albumin in birds according to micro-complement fixation analysis. J Mol Evol 3:243–262
Prager EM, Welling GW, Wilson AC (1978a) Comparison of various immunological methods for distinguishing among mammalian pancreatic ribonucleases of known amino acid sequence. J Mol Evol 10:293–307
Prager EM, Wilson AC, Périn J-P, Jollès P (1978b) Further studies of an anomalous cross-reaction involving worm and vertebrate lysozymes. Immunochemistry 15:577–583
Prager EM, Wilson AC (1971a) The dependence of immunological cross-reactivity upon sequence resemblance among lysozymes. 1. Micro-complement fixation studies. J Biol Chem 246:5978–5989
Prager EM, Wilson AC (1971b) The dependence of immunological cross-reactivity upon sequence resemblance among lysozymes. II. Comparison of precipitin and microcomplement fixation results. J Biol Chem 246:7010–7017
Prager EM, Wilson AC (1993) Information content of immunological distances. Meth Enzymol 224:140–152
Romero-Herrera AE, Lehmann H, Castillo O (1976) The primary structure of the myoglobin of rabbit (Oryctolagus cuniculus). Biochim Biophys Acta 439:51–54
Swanson KW, Irwin DM, Wilson AC (1991) Stomach lysozyme gene of the langur monkey: tests for convergence and positive selection. J Mol Evol 33:418–425
Wallace DG, Boulter D (1976a) Immunological comparisons of higher plant plastocyanins. Phytochemistry 15:137–141
Wallace DG, Boulter D (1976b) The sequence-immunology correlation among higher plant plastocyanins. Immunochemistry 13:831–835
Wang C-C, Avila R, Jones BN, Gurd FRN (1977) Complete primary structure of the major component myoglobin of Pacific common dolphin (Delphinus delphis). Biochemistry 16:4978–4981
Weinstock J, Baldwin GS (1988) Nucleotide sequence of porcine liver albumin. Nucleic Acids Res 16:9045
Wilson AC, Carlson SS, White TJ (1977) Biochemical evolution. Annu Rev Biochem 46:573–639
Yeh TC, Wilson AC, Irwin DM (1993) Evolution of rodent lysozymes: isolation and sequence of the rat lysozyme genes. Mol Phylo Evol 2:65–75
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Prager, E.M. The sequence-immunology correlation revisited: Data for cetacean myoglobins and mammalian lysozymes. J Mol Evol 37, 408–416 (1993). https://doi.org/10.1007/BF00178870
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00178870