SUMMARY: Eight yeast species (the ascomycetes , , , , and , and the imperfect yeasts and ) have been compared with respect to the proteins solubilized by glucanase treatment of amino-acid-labelled, purified walls. Except for , a significant quantity of radioactively labelled protein material was liberated by this treatment. Among the major protein components solubilized was a material larger than 100 kDa (heterogeneous in size in some species) and a molecule ranging in size from 31.5 to 34 kDa depending on the yeast species. The large material was of glycoprotein nature, with the sugar portion -glycosidically linked to the protein moiety; in some species, this material did not bind concanavalin A (ConA), indicating the presence of terminal sugar residues different from mannose, glucose or glucosamine. The form of 31.5-34 kDa was present in all the species studied except ; it was a mannoprotein, except in , which possessed a 31.5 kDa form not sensitive to tunicamycin or endoglycosidase H and not recognized by ConA. Antigenic cross-reactivity was observed between the protein moieties of the 33 kDa form of and the species of equivalent size in and . Similar partial proteolysis patterns were obtained for the 33 kDa form of and the 34 kDa forms of and .


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