Abstract
The alpha, gamma and delta races of Colletotrichum lindemuthianum secrete endopolygalacturonases which behave in an identical manner during purification on several columnn materials. The endopolygalacturonase secreted by each of these races is completely inhibited by proteins associated with the cell walls of the Red Kidney, Small White and Pinto varieties of the true bean ( Phaseolus vulgaris). These three bean varieties differ in their response to the alpha, gamma and delta races of the pathogen. Crude extracts from the hypocotyl cell walls of each of the bean varieties possess approximately equal abilities to inhibit each of the endopolgalacturonases. The proteins from Red Kidney and Pinto beans, which inhibit the endopolygalacturonase, purify identically, and the purified protein preparations possess equal specific activities. These proteins, purified for their ability to inhibit the endopoly-galacturonase secreted by the alpha race, are equally able to inhibit the endopolygalacturonases from the gamma and delta races. The purified endopolygalacturonases from the three C. lindemuthianum races compete equally for inhibitor. It is concluded that the endopolygalacturonases secreted by the three races of C. lindemuthianum are identical, and that their inhibitor proteins present in the three bean varieties are also identical.
Published Version
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