Characterization and oxidative in vitro cross-linking of an extensin-like protein and a proline-rich protein purified from chickpea cell walls.
Two cell wall proteins from chickpea, known to be rapidly insolubilised by an elicitor-stimulated oxidative burst in-vivo, were purified from suspension cells. N-terminal protein sequencing revealed them as a proline-rich protein and an extensin-like protein. Oxidative cross-linking could be modelled in an in vitro system utilising horseradish peroxidase, H2O2 and the substrate proteins.
Otte
O
O
Institut für Biochemie und Biotechnologie der Pflanzen, Westfälische Wilhelms-Universität, Münster, Germany.
Barz
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W
D002462:Cell Membrane / Q000737:chemistry; D003432:Cross-Linking Reagents / Q000737:chemistry*; D007887:Fabaceae / Q000737:chemistry*; D006023:Glycoproteins / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000494:pharmacology; D006861:Hydrogen Peroxide / Q000494:pharmacology; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D010946:Plants, Medicinal; D011392:Proline / Q000737:chemistry*
D003432:Cross-Linking Reagents; D006023:Glycoproteins; D010940:Plant Proteins; C005488:extensin protein, plant; D011392:Proline; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase