Abstract
SUMMARYTwo major groups of heat-stable proteins have been purified by heat denaturation from homogenates of eggs of the potato-cyst nematodes Globodera rostochiensis and G. pallida. SDS-polyacrylamide gel electrophoresis of protein homogenates from 6 G. rostochiensis populations and 7 G. pallida populations revealed 2 bands specific for G. rostochiensis and 3 bands specific for G. pallida. Two-dimensional electrophoresis showed that the 2 bands specific for G. rostochiensis consisted of 2 polypeptides differing slightly in isoelectric point, as did one of the bands specific for G. pallida. Conventional antisera made against protein homogenates of either Globodera species showed a complete cross-reaction with the species-specific proteins. The perspectives of the differences in protein composition between G. rostochiensis and G. pallida, established in this study, for a quantitative differentiation of mixed field populations of the two Globodera species, involving monoclonal antibodies, are discussed.
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