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 in | Physiological and molecular plant pathology Vol. 37; no. 3; pp. 193 - 206 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
London
Elsevier India Pvt Ltd
1990
Elsevier |
Subjects | |
Online Access | Get full text |
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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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0885-5765 1096-1178 |
DOI: | 10.1016/0885-5765(90)90011-L |