Abstract
Polygalacturonase-inhibiting proteins (PGIPs) are believed to be one component of plants inherent defense mechanisms against fungal pathogens. We have purified a PGIP from mature grapefruit (Citrus paradisi cv. Marsh) flavedo using ammonium sulfate precipitation, preparative isoelectric focusing and ion exchange chromatography. Two peaks of PGIP activity were separated by isoelectric focusing, one at pH 6–7 and one at pH 9–10. The basic protein was more abundant than the neutral protein and was selected for further purification. The basic protein binds to S Sepharose at pH 6.1 and has an apparent Mr of ≈43,000 based on SDS-PAGE analysis. The protein is glycosylated as revealed by binding to ConA sepharose and is serologically similar to PGIPs from bean hypocotyl and pear fruit. Two dimensional PAGE analysis revealed the presence of two bands of similar Mr but with slightly different pIs (≈9.0–9.5). The N-terminal amino acid sequence of grapefruit PGIP shows high homology with PGIPs from fruit of other species and with a cDNA clone of PGIP that was isolated from a Citrus sinensis cv. Hamlin expression library. Grapefruit PGIP inhibits polygalacturonases from Aspergillus niger, and the citrus pathogen Penicillium italicum. We are interested in the role of PGIP in resistance of citrus fruit to postharvest decay fungi.
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