Isolation of a polygalacturonase-inhibiting protein (PGIP) from wheat.
Evidence for the presence of a polygalacturonase-inhibiting protein (PGIP) from a monocotyledonous cereal is presented. A 40.3-kDa PGIP that was closely associated with the cell wall was acetone-extracted and purified from wheat (Triticum aestivum L.) leaves and stems. Wheat PGIP exhibited a highly selective inhibitory activity against endopolygalacturonase (EPG) from various fungi. Of nine EPG tested, wheat PGIP only inhibited EPG from Cochliobolus sativus, a pathogen of the tribe Poaceae. A short N-terminal amino acid sequence of wheat PGIP shows no similarity to any other characterized PGIP.
Kemp
Gabré
G
Department of Plant Sciences, University of the Free State, PO Box 339, Bloemfontein 9300, South Africa. gabre@ccrc.uga.edu
Bergmann
Carl W
CW
Clay
Ron
R
Van der Westhuizen
Amie J
AJ
Pretorius
Zacharias A
ZA
D000935:Antifungal Agents / Q000302:isolation & purification* / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000302:isolation & purification*; D005658:Fungi / Q000145:classification / Q000187:drug effects*; D015151:Immunoblotting; D008163:Luminescent Measurements; D008826:Microbial Sensitivity Tests; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D011096:Polygalacturonase / Q000037:antagonists & inhibitors*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014908:Triticum / Q000502:physiology*
D000935:Antifungal Agents; D004791:Enzyme Inhibitors; C081479:PGIP protein, plant; D010940:Plant Proteins; D011096:Polygalacturonase