Abstract

Lilium longiflorum possesses several advantages for investigating the nature of self-incompatibility. The large hollow styles permit analyses of proteins and enzymes from pollen tubes removed from the styles after selfing or crossing along with their corresponding styles, as well as from pollen grains and from styles of unpollinated flowers. Biochemical methods have been developed for protein extractions and subsequent analyses by disc electrophoresis. These techniques have been used to demonstrate changing protein and esterase patterns in pollen and styles from four cultivars. No apparent association between the self-incompatibility reaction and proteins which migrate at pH 8.3 in 71/2% acryamide gel was noted. These analyses included soluble proteins, esterases, peroxidases and several dehydrogenases.

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