Skip to main content
Log in

Separation and localization of two classes of auxin binding sites in corn coleoptile membranes

  • Published:
Planta Aims and scope Submit manuscript

Summary

Further evidence is presented for the discrete nature of the two classes of high affinity auxin binding sites in corn (Zea mays L.) coleoptile membranes, site 1 and site 2. Fractions can be obtained by differential centrifugation that exhibit binding kinetics characteristic of site 2, but not site 1. Membrane preparations containing both binding sites may be resolved on sucrose gradients into a light and a heavy band, whose binding kinetics and analogue binding specificities correspond to those deduced for site 1 and site 2 respectively in unfractionated membranes. Evidence from enzymic and chemical assays and from electron microscopy suggests that site 2, the auxin-specific binding site, is located in fractions enriched in plasma membrane, whereas site 1 is associated with Golgi membranes and/or endoplasmic reticulum.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

NAA:

1-naphthylacetic acid

IAA:

3-indolylacetic acid

TIBA:

2,3,5-triiodobenzoic acid

SDH:

succinic dehydrogenase

IDPase:

inosine diphosphatase

References

  • Batt, S., Wilkins, M.B., Venis, M.A.: Auxin binding to corn coleoptile membranes: kinetics and specificity. Planta (Berl.) 130, 7–13 (1976)

    Google Scholar 

  • Folch, J., Lees, M., Sloane-Stanley, G.H.: A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226, 497–509 (1957)

    PubMed  Google Scholar 

  • Gawlik, S.R., Shen-Miller, J.: Effects of indoleacetic acid on dicytosomes of apical and expanding cells of oat coleoptiles. Plant Physiol. 54, 217–221 (1974)

    Google Scholar 

  • Hertel, R., Thomson, K., Russo, V.E.A.: In vitro auxin binding to particulate cell fractions from corn coleoptiles. Planta (Berl.) 107, 325–340 (1972)

    Google Scholar 

  • Hodges, T.K., Leonard, R.T.: Purification of a plasma-membranebound adenosine triphosphatase from plant roots. In: Methods in Enzymology XXXII, pp. 392–406. Fleischer, S., Packer, L. (eds) New York-San Francisco-London: Academic Press 1974

    Google Scholar 

  • Hodges, T.K., Leonard, R.T., Bracker, C.E., Keenan, T.W.: Purification of an ionstimulated adenosine trophosphatase from plant roots:association with plasma membranes. Proc. Nat. Acad. Sci. U.S.A. 69, 3307–3311 (1972)

    PubMed  Google Scholar 

  • Leigh, R.A., Williamson, F.A., Wyn-Jones, G.: Presence of two different membrane bound, KCl-stimulated adenosine triphosphatase activities in maize roots. Plant Physiol. 55, 678–685 (1975)

    Google Scholar 

  • Leonard, R.T., Hansen, D., Hodges, T.K.: Membrane-bound adenosine triphosphatase activities of oat roots. Plant Physiol. 51, 749–754 (1973)

    Google Scholar 

  • Lowry, O.N., Lopez, J.H.: The determination of inorganic phosphate in the presence of labile phosphate esters. J. Biol. Chem. 162, 421–428 (1946)

    Google Scholar 

  • Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, K.J.: Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 262–275 (1951)

    Google Scholar 

  • Pennington, R.J.: Biochemistry of dystrophic muscle. Mitochondrial succinate-tetrazolium reductase and adenosine triphosphatase. Biochem. J. 80, 649–654 (1961)

    PubMed  Google Scholar 

  • Powell, J.T., Brew, K.: Glycosyltransferases in the Golgi membranes of onion stem. Biochem. J. 142, 203–209 (1974)

    PubMed  Google Scholar 

  • Ray, P.M., Shininger, T.L., Ray, M.M.: Isolation of β-glucan synthetase particles from plant cells and ientification with Golgi membranes. Proc. Nat. Acad. Sci. USA 64, 605–612 (1969)

    Google Scholar 

  • Roland, J.C., Lembi, C.A., Morre, D.J.: Phosphotungstic acid-chromic acid as a selective electron-dense stain for plasma membranes of plant cells. Stain Technology 47, 195–200 (1972)

    PubMed  Google Scholar 

  • Rouser, G., Siakotoj, A.N., Fleischer, S.: Quantitative analysis of phospholipids by thinlayer chromatography and phosphorus analysis of spots. Lipids 1, 85–86 (1966)

    Google Scholar 

  • Stadtman, T.C.: Preparation and assay of cholesterol and ergosterol. In: Methods in Enzymology III, pp 392–394, Colowick, S.P., Kaplan, N.O. (eds) New York: Academic Press 1957

    Google Scholar 

  • Van der Woude, W.J., Lembi, C.A., Morre, D.J., Kindinger, J.I., Ordin, L.: β-Glucansynthetases of plasma membrane and Golgi apparatus from onion stem. Plant Physiol. 54, 333–340 (1974)

    Google Scholar 

  • Wilkinson, G.: Statistical estimations in enzyme kinetics. Biochem. J. 80, 324–332 (1961)

    PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Batt, S., Venis, M.A. Separation and localization of two classes of auxin binding sites in corn coleoptile membranes. Planta 130, 15–21 (1976). https://doi.org/10.1007/BF00390839

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00390839

Keywords

Navigation