This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Web of Science (137) Citing Articles via Google Scholar Google Scholar Articles by Ray, P. M. Articles by Hertel, R. Search for Related Content PubMed PubMed Citation Articles by Ray, P. M. Articles by Hertel, R. Agricola Articles by Ray, P. M. Articles by Hertel, R.

Articles

Characterization of Naphthaleneacetic Acid Binding to Receptor Sites on Cellular Membranes of Maize Coleoptile Tissue ¹

Rainer Hertel^b

^a Department of Biological Sciences, Stanford University, Stanford, California 94305, ^b Institut fur Biologie III, Universität Freiburg i. Br., D-7800 Freiburg, German Federal Republic

Characteristics of and optimum conditions for saturable ("specific") binding of [¹⁴C]naphthaleneacetic acid to sites located on membranous particles from maize (Zea mays L.) coleoptiles are described. Most, if not all, of the specific binding appears to be due to a single kinetic class of binding sites having a K_D of 5 to 7 x 10^–7M for naphthalene-1-acetic acid (NAA). Binding of NAA is insensitive to high monovalent salt concentrations, indicating that binding is not primarily ionic. However, specific binding is inhibited by Mg²⁺ or Ca²⁺ above 5 mM. Specific binding is improved by organic acids, especially citrate. Binding is heat-labile and is sensitive to agents that act either on proteins or on lipids. Specific binding is reversibly inactivated by reducing agents such as dithioerythritol; a reducible group, possibly a disulfide group, may be located at the binding site and required for its function. The affinity of the specific binding sites for auxins is modified by an unidentified dialyzable, heat-stable, apparently amphoteric, organic factor ("supernatant factor") found in maize tissue.

This article has been cited by other articles:

				P. Campanoni and P. Nick Auxin-Dependent Cell Division and Cell Elongation. 1-Naphthaleneacetic Acid and 2,4-Dichlorophenoxyacetic Acid Activate Different Pathways Plant Physiology, March 1, 2005; 137(3): 939 - 948. [Abstract] [Full Text] [PDF]

				J. M. Bauly, I. M. Sealy, H. Macdonald, J. Brearley, S. Dröge, S. Hillmer, D. G. Robinson, M. A. Venis, M. R. Blatt, C. M. Lazarus, et al. Overexpression of Auxin-Binding Protein Enhances the Sensitivity of Guard Cells to Auxin Plant Physiology, November 1, 2000; 124(3): 1229 - 1238. [Abstract] [Full Text]

				N. Leblanc, K. David, J. Grosclaude, J.-M. Pradier, H. Barbier-Brygoo, S. Labiau, and C. Perrot-Rechenmann A Novel Immunological Approach Establishes That the Auxin-binding Protein, Nt-abp1, Is an Element Involved in Auxin Signaling at the Plasma Membrane J. Biol. Chem., October 1, 1999; 274(40): 28314 - 28320. [Abstract] [Full Text] [PDF]

				G. GARDNER Azidoatrazine: Photoaffinity Label for the Site of Triazine Herbicide Action in Chloroplasts Science, February 27, 1981; 211(4485): 937 - 940. [Abstract] [PDF]

				K. David, E. Carnero-Diaz, N. Leblanc, M. Monestiez, J. Grosclaude, and C. Perrot-Rechenmann Conformational Dynamics Underlie the Activity of the Auxin-binding Protein, Nt-abp1 J. Biol. Chem., September 7, 2001; 276(37): 34517 - 34523. [Abstract] [Full Text] [PDF]