Purification and Properties of Membrane-Bound Auxin Receptors in Corn

  • M. A. Venis
Conference paper
Part of the Proceedings in Life Sciences book series (LIFE SCIENCES)


Binding sites in corn coleoptile membranes with high affinity for auxins were first detected by Hertel et al. (1). Subsequently we reported evidence for two kinetic classes of auxin binding sites (2,3) and described their solubilization and partial purification (4). Other workers could distinguish only a single kinetic class of binding sites, either in the membrane-bound (5) or solubilized state (6). On the other hand, Dohrmann et al. (7) have suggested that there are three types of auxin-binding sites, two of which have affinities for 1-naphthylacetic acid (NAA) comparable to those reported by ourselves. The third site, which preferentially binds 2,4-dichlorophenoxyacetic acid (2,4-D) and may be an auxin transport site (8), is only revealed under specialized assay conditions.


Auxin Binding Acetone Powder Extract Corn Membrane Supernatant Factor Chromatographic Purification Method 
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  1. 1.
    Hertel, R., Thomson, K., Russo, V.E.A.: Planta 107, 325–340 (1972)CrossRefGoogle Scholar
  2. 2.
    Batt, S., Wilkins, M.B., Venis, M.A.: Planta 130, 7–13 (1976)CrossRefGoogle Scholar
  3. 3.
    Batt, S., Venis, M.A.: Planta 130, 15–21 (1976)CrossRefGoogle Scholar
  4. 4.
    Venis, M.A.: Nature (Lond.) 266, 268–269 (1977)CrossRefGoogle Scholar
  5. 5.
    Ray, P.M., Dohrmann, U., Hertel, R.: Plant Physiol. 59, 357–364 (1977)PubMedCrossRefGoogle Scholar
  6. 6.
    Cross, J.W., Briggs, W.R.: Plant Physiol. 62, 152–157 (1978)PubMedCrossRefGoogle Scholar
  7. 7.
    Dohrmann, U., Hertel, R., Kowalik, H.: Planta 140, 97–106 (1978)CrossRefGoogle Scholar
  8. 8.
    Jacobs, M., Hertel, R.: Planta 142, 1–10 (1978)CrossRefGoogle Scholar
  9. 9.
    Venis, M.A., Watson, P.J.: Planta 142, 103–107 (1978)CrossRefGoogle Scholar
  10. 10.
    Molinari, A.M., Medici, N., Moncharmont, B., Puca, G.A.: Proc. Natl. Acad. Sci USA 74, 4886–4890(1977)PubMedCrossRefGoogle Scholar
  11. 11.
    Porath, J., Carlsson, J., Olssen, I., Beifrage, G.: Nature (Lond.) 258, 598–599 (1975)CrossRefGoogle Scholar
  12. 12.
    Lowry, O.H., Rosebrough, J.J., Farr, A.L., Randall, R.J.: J. Biol. Chem. 193, 265–275 (1951)PubMedGoogle Scholar
  13. 13.
    O’Brien, T.J., Liebke, H.H., Cheung, H.S., Johnson, L.K.: Anal. Biochem. 72, 38–44 (1976)PubMedCrossRefGoogle Scholar
  14. 14.
    Kopcewicz, J., Ehmann, A., Bandurski, R.S.: Plant Physiol. 54, 846–851 (1974)PubMedCrossRefGoogle Scholar
  15. 15.
    Venis, M.A.: Plant Physiol. 49, 24–27 (1972)PubMedCrossRefGoogle Scholar
  16. 16.
    Gordon, S.A., Weber, R.P.: Plant Physiol. 26, 192–195 (1951)PubMedCrossRefGoogle Scholar
  17. 17.
    Hager, A., Menzel, H., Krauss, A.: Planta 100, 47–75 (1971)CrossRefGoogle Scholar
  18. 18.
    Cross, J.W., Briggs, W.R., Dohrmann, U.C., Ray, P.M.: Plant Physiol. 61, 581–584 (1978)PubMedCrossRefGoogle Scholar
  19. 19.
    Ray, P.M., Dohrmann, U., Hertel, R.: Plant Physiol. 60, 585–591 (1977)PubMedCrossRefGoogle Scholar
  20. 20.
    Klun, J.A., Tipton, C.L., Robinson, J.F., Ostrem, D.L., Beroza, M.: J. Agric. Food Chem. 18, 663 – 665 (1970)CrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1980

Authors and Affiliations

  • M. A. Venis
    • 1
  1. 1.Shell Biosciences LaboratorySittingbourne Research CentreSittingbourne, KentUK

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