Partial purification and characterization of a gibberellin-binding protein from seedlings of Azukia angularis

Biochem Biophys Res Commun. 1997 Dec 29;241(3):782-6. doi: 10.1006/bbrc.1997.7896.

Abstract

Little is known about mechanisms for the perception of gibberellin (GA), a phytohormone, by plants. A GA-binding protein (GBP) with receptor-like characteristics was partially purified from azuki bean (Azukia angularis) seedlings. Gibberellins that caused much elongation of azuki epicotyl sections showed strong binding affinity for the GBP, and their biosynthetic precursors and inactive metabolites had weak affinity for it. The apparent Kd value for GA4 was calculated to be 7 x 10(-10) M from Scatchard plots. The molecular weight of the GBP in the native state was estimated to be 25,000 by high-performance liquid chromatography with a gel-permeation column. The GBP may be one of the receptor candidates for GAs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / chemistry*
  • Carrier Proteins / isolation & purification*
  • Chromatography, Gel
  • Fabaceae
  • Gibberellins / metabolism*
  • Gibberellins / pharmacology
  • Hydrogen-Ion Concentration
  • Kinetics
  • Molecular Weight
  • Phosphoproteins / chemistry*
  • Phosphoproteins / isolation & purification*
  • Plant Proteins / chemistry*
  • Plant Proteins / isolation & purification*
  • Plants, Medicinal
  • Protein Binding
  • Seeds / chemistry

Substances

  • Carrier Proteins
  • Gibberellins
  • Phosphoproteins
  • Plant Proteins
  • gibberellin-binding phosphoprotein, plant