Evolution of Aldehyde Reductase: An Immunological Approach to the Relatedness of Aldehyde Reductase from Different Species

  • W. S. Davidson
  • T. G. Flynn


Antisera to aldehyde reductase from fruit-fly (Drosophila melanogaster) and chicken were cross-reacted with aldehyde reductase from several species of insects and birds using the technique of microcomplement fixation. Large differences in immunological distances are evident between species of the Class Insecta and of the Class Ayes indicating considerable differences in the amino acid sequences of the aldehyde reductase of these species. Immunological distances for aldehyde reductase between pairs of insect species or bird species when plotted against the immunological distances for transferrin, albumin, lysozyme and α-glycerophosphate dehydrogenase for the same pairs of species gave a linear relationship in each case. From these relationships the rate of evolution of aldehyde reductase in terms of a unit evolutionary period (UEP) was calculated to be 12 which agreed favorably with the value previously obtained from compositional comparisons. A UEP of 12 is approximately half that of lactate dehydrogenase and shows that aldehyde reductase is evolving at twice the rate of glycolytic enzymes. This may indicate a relatively non-essential metabolic role for the enzyme.


Bird Species Guinea Fowl Glycerol Dehydrogenase Aldehyde Reductase Compositional Relatedness 
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  1. Arnheim, N. and Wilson, A. C., 1967, Quantitative immunological comparison of bird lysozymes, J. Biol. Chem. 242:3951–3956.Google Scholar
  2. Borror, D. J., Delong, D. M. and Triplehorn, C.A., 1976, “Introduction to the Study of Insects,” IVth edition, Holt, Reinhart and Winston.Google Scholar
  3. Champion, A. B., Prager, E. M., Wachter, D. and Wilson, A. C., 1974, Microcomplement fixation, in: “Biochemical and Immunological Taxonomy of Animals,” C. A. Wright, ed., Academic Press, New York.Google Scholar
  4. Champion, A. B., Soderberg, K. L., Wilson, A. C. and Ambler, R. P., 1975, Immunological comparison of azurius of known amino acid sequence: dependency of cross-reactivity upon sequence resemblance, J. Molec. Evol. 5:291–305.Google Scholar
  5. Collier, G. E. and MacÌntyre, R. J., 1977, Microcomplement fixation studies on the evolution of a-glycerophosphate dehydrogenase within the genus Drosophila, Proc. Nat. Acad. Sci. 74: 684–688.PubMedCrossRefGoogle Scholar
  6. Davidson, W.S. and Flynn, T.G., 1979a, Kinetics and mechanism of action of aldehyde reductase from pig kidney, Biochem. J., 177:595–601.Google Scholar
  7. Davidson, W. S. and Flynn, T. G., 1979b, A functional arginine residue in NADPH-dependent aldehyde reductase from pig kidney, J. Biol. Chem.,254:3724–3479.Google Scholar
  8. Davidson, W. S. and Flynn, T. G., 1979c, Compositional relatedness of aldehyde reductase from several species, J. Molec. Evol. in press.Google Scholar
  9. Davidson, W. S., Walton, D. J. and Flynn, T. G., 1978, A comparative study of the tissue and species distribution of ANDPH-dependent aldehyde reductase., Comp. Biochem. Physiol. 60B:309–315.Google Scholar
  10. Felsted, R. L., Gee, M. and Bachur, N. R., 1974, Rat liver daunorubicin reductase: an aldoketo reductase, J. Biol. Chem. 249:3672–3678.Google Scholar
  11. Flynn, T. G., Shires, J. and Walton, D. J., 1975, Properties of the NADPH-dependent aldehyde reductase from pig kidney: amino acid composition, reactivity of cysteinyl residues and stereochemistry of D-glyceraldehyde reduction., J. Biol Chem., 250: 2933–2940.PubMedGoogle Scholar
  12. Ibrahimi, I. M., Prager, E. M., White, T. J. and Wilson, A. C., 1979, Amino acid sequence of California Quail Lysozyme. Effect of evolutionary substitutions on the antigenic structure of lysozyme, Biochemistry 18: 2736–2744.Google Scholar
  13. Kormann, A. W., Hurst, R. O. and Flynn, T. G., 1972, Purification and properties of an NADP+-dependent glycerol dehydrogenase from rabbit skeletal muscle, Biochim. Biophys. Acta., 258:40–55.Google Scholar
  14. Metzger, H., Shapiro, M. B., Mosimann, J. E. and Vinton, J. E., 1968, Assessment of compositional relatedness between proteins, Nature 219: 1166–1168.Google Scholar
  15. Prager, E. M., Brush, A. H., Nolau, R. A., Nakanishi, M. and Wilson, A. C., 1974, Slow evolution of transferrin and albumin in birds according to micro-complement fixation analysis, J. Molec. Evol. 3:243–262.Google Scholar
  16. Prager, E. M. and Wilson, A. C., 1979, Phylogenetic relationships and rates of evolution in birds, Proc. Int. Ornith. Congr. 17: in press.Google Scholar
  17. Sheaff, C. M. and Doughty, C. C., 1976, Physical and kinetic properties of homogeneous bovine lens aldose reductase, J. Biol. Chem. 251:2696–2702.PubMedGoogle Scholar
  18. Wermuth, B., Munch, J. D. B. and von Wartburg, J. P. 1977, Tion and properties of NADPH-dependent aldehyde human liver, J. Biol. Chem. 252:3821–3828.PubMedGoogle Scholar
  19. Wilson, A. C., Carlson, S. C. and White, J. T., 1977, evolution, Ann. Rev. Biochem. 46:572–639. 1977, Purifica-reductase from BiochemicalCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1980

Authors and Affiliations

  • W. S. Davidson
    • 1
    • 2
  • T. G. Flynn
    • 1
    • 2
  1. 1.Department of BiochemistryUniversity of CaliforniaBerkeleyUSA
  2. 2.Queen’s UniversityKingstonCanada

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