A comparison of the biochemical and physiological properties of a polygalacturonase from two races of Colletotrichum lindemuthianum

An endo-glycolytic polygalacturonase [EC 3·2·1·15] was purified to homogeneity from culture filtrates of Colletotrichum lindemuthianum races beta and gamma. The molecular weights (c. 39000), pls (9·4), N-terminal amino acid sequences, amino acid compositions, specific activities and the substrate ut...

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Published inPhysiological and molecular plant pathology Vol. 37; no. 3; pp. 193 - 206
Main Authors Keon, John P.R., Waksman, Gabriel, Bailey, John A.
Format Journal Article
LanguageEnglish
Published London Elsevier India Pvt Ltd 1990
Elsevier
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Summary:An endo-glycolytic polygalacturonase [EC 3·2·1·15] was purified to homogeneity from culture filtrates of Colletotrichum lindemuthianum races beta and gamma. The molecular weights (c. 39000), pls (9·4), N-terminal amino acid sequences, amino acid compositions, specific activities and the substrate utilization of the enzymes were indistinguishable. Hypocotyl tissues from cultivars of Phaseolus vulgaris, that differed in their resistance and susceptibility to races beta and gamma of C. lindemuthianum, were all rapidly macerated and killed by endopolygalacturonase from both races of fungus. These data suggest that the biochemical and physiological properties of the endopolygaiacturonase produced by C. lindemuthianum cannot explain the cultivar specificity exhibited by different races of this pathogen.
Bibliography:ObjectType-Article-1
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ISSN:0885-5765
1096-1178
DOI:10.1016/0885-5765(90)90011-L