SUMMARY: Purification of the sexual agglutinins of both mating types of (= syngen II) was achieved by a three-step procedure. Electron microscopy showed both agglutinins to be long, linear molecules. The mt agglutinin was a rigid molecule with one bulbous end and an average length of 251 nm. The mtagglutinin was longer (average length 349 nm), had a more flexible conformation and lacked a bulbous end. The was estimated to be 1·0 × 10 for the mt and 1·2 × 10 for the mt agglutinin. The mt agglutinin had a very high content of hydroxyproline (41%) and serine (14%); the mt agglutinin had a high content of glycine, serine and hydroxyproline (18, 16 and 12%, respectively). The main sugars in the agglutinins of both mating types were arabinose and galactose. The carbohydrate portion represented about 40% of the in both agglutinins. The biological activity of both agglutinins could be destroyed by periodate treatment (although their sensitivities differed), indicating the involvement of carbohydrate residues. A differential susceptibility for exoglycosidases was observed: enzymic removal of terminal glucose residues abolished the biological activity of the mt agglutinin only, while removal of mannose residues selectively inactivated the mt agglutinin. The similarities in form and composition of the agglutinins of several species suggest that these recognition molecules have a common ancestry, and that the species barriers are at least partially dependent on differences in the carbohydrate side-chains.


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