SUMMARY: The killer toxin KT 28 of strain 28 is primarily bound to the mannoprotein of the cell wall of sensitive yeasts. The mannoprotein of X 2180 was purified; gel filtration and SDS-PAGE indicated an estimated of 185000. The ability to bind killer toxin KT 28 increased during purification of the mannoprotein. Removing the protein part of the mannoprotein by enzymic digestion or removing the alkali-labile oligosaccharide chains by β-elimination did not destroy the ability to bind killer toxin KT 28. However, binding activity was lost when the 1,6-α-linkages of the outer carbohydrate backbone were hydrolysed by acetolysis. The separated oligomannosides of the side chains also failed to bind toxin, indicating that the main mannoside chains were essential for the receptor activity. The reversible adsorption of killer toxin to mannoprotein was demonstrated by linking it covalently to Sepharose and using this material for affinity chromatography. A 90-fold increase in the specific activity of a preparation of killer toxin KT 28 was achieved in this way.


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