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Yeast cell wall proteins, including Cwp1p and α-agglutinin, could be released by treating the cell wall with either β-1,3- or β-1,6-glucanases, indicating that both polymers are involved in anchoring cell wall proteins. It was shown im-munologically that both β-1,3- and β-1,6-glucan were linked to yeast cell wall proteins, including Cwp1p and α-agglutinin. It was further shown that β-1,3-glucan was linked to the wall protein through a β-1,6-glucan moiety. The β-1,6-glucan moiety could be removed from Cwp1p and other cell wall proteins by cleaving phosphodiester bridges either enzymatically using phosphodiesterases or chemically using ice-cold aqueous hydrofluoric acid. These observations are consistent with the notion that cell wall proteins in Saccharomyces cerevisiae are linked to a β-1,3-/β-1,6-glucan heteropolymer through a phosphodiester linkage and that this polymer is responsible for anchoring cell wall proteins. It is proposed that this polymer is identical to the alkali-soluble β-1,3-/β-1,6-glucan heteropolymer characterized by Fleet and Manners (1976,1977). [ABSTRACT FROM PUBLISHER]