Summary: The peptides of the hyphal wall of have been studied to determine their physical characteristics. We have removed these peptides from the wall by treatment with 0·5 M-NaOH and shown by DEAE cellulose chromatography that there are five major fractions present. Amino acid analysis showed distinct differences in primary structure between these fractions but similarities in the proportions of hydrophilic residues and the ratios of basic residues to acidic residues of each fraction. Two unknown compounds, one acidic and the other basic, were also detected.

Extraction of the wall with NHOH released a high molecular weight glycopep-tide complex, from which the peptides were released with NaOH. -Glycosyl serine linkages were demonstrated to occur within this complex.

Enzyme digestion of either the chitin or the β-1,3-polymer of the hyphal wall failed to release peptide material. This, together with the above, suggests that the glycopeptide of the hyphal wall is a highly ordered structure of peptides joined by a branched carbohydrate linker of unknown composition, and that it is not demonstrably covalently linked to the other major components of the wall. It probably occurs as an extremely large structure embedded in the other polymers of the hyphal wall.


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