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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.
The hydroxyproline-rich root nodules of legumes provide a microaerobic niche for symbiotic nitrogen-fixing Rhizobacteria. The contributions of the cell wall and associated structural proteins, particularly the hydroxyproline-rich glycoproteins (HRGPs), are therefore of interest. Our approach involved identification of the protein components by direct chemical analysis of the insoluble wall. Chymotryptic...
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