Evidence for specific, high-affinity binding sites for a proteinaceous elicitor in tobacco plasma membrane

FEBS Lett. 1995 Oct 30;374(2):203-7. doi: 10.1016/0014-5793(95)01108-q.

Abstract

Binding of cryptogein, a proteinaceous elicitor, was studied on tobacco plasma membrane. The binding of the [125I]cryptogein was saturable, reversible and specific with an apparent Kd of 2 nM. A single class of cryptogein binding sites was found with a sharp optimum pH for binding at about pH 7.0. The high-affinity correlates with crytogein concentrations required for biological activity in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algal Proteins*
  • Binding Sites
  • Cell Membrane / metabolism
  • Fungal Proteins / metabolism*
  • Kinetics
  • Plants, Toxic*
  • Tobacco / metabolism*

Substances

  • Algal Proteins
  • Fungal Proteins
  • cryptogein protein, Phytophthora cryptogea