1887

Abstract

The extracellular killer toxin of strain 28 was concentrated by ultrafiltration of culture supernatants and purified by ion-exchange chromatography. Polyacrylamide gradient gel electrophoresis in SDS indicated that the toxin is a glycoprotein with a molecular weight of about 16000. Amino acid analysis revealed that the killer toxin contains 111 amino acid residues, equivalent to a molecular weight of 14045; the ratio of protein to carbohydrate in the molecule is therefore about 9 to 1. The isoelectric point of the killer toxin was pH 4·4 to 4·5. The toxin was unaffected by heating at 40 °C for 1 h and its maximum activity against sensitive yeast cells was observed at pH 5v0. Cell-free extracts prepared from well-washed cells of strain 28 were toxic for sensitive yeasts. The toxin present in these extracts (intracellular toxin) was partially purified by ultrafiltration and ion-exchange chromatography. The isoelectric points of the extracellular and intracellular killer toxin were similar.

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1982-11-01
2024-05-01
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