Evidence for specific, high-affinity binding sites for a proteinaceous elicitor in tobacco plasma membrane.
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.
Wendehenne
D
D
Unité associée INRA/Université de Bourgogne 692, INRA, Dijon, France.
Binet
M N
MN
Blein
J P
JP
Ricci
P
P
Pugin
A
A
D020418:Algal Proteins; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism*; D007700:Kinetics; D010947:Plants, Toxic; D014026:Nicotiana / Q000378:metabolism*
D020418:Algal Proteins; D005656:Fungal Proteins; C061032:cryptogein protein, Phytophthora cryptogea