Immunochemical analysis of the carbohydrate moiety of yeast killer toxin K28

✍ Scribed by Manfred J. Schmitt; Peter C. Pfeiffer

• Publisher: Springer Netherlands
• Year: 1990
• Tongue: English
• Weight: 546 KB
• Volume: 58
• Category: Article
• ISSN: 0003-6072
• DOI: 10.1007/bf00399340

✦ Synopsis

Killer toxin K28, a 16 kd protein secreted by the wine yeast Saccharomyces cerevisiae strain 28, was reversibly bound by a column of Concanavalin A-Sepharose, confirming its glycoprotein nature. HPLC analysis of acid hydrolyzates of K28 toxin as well as Western-blots of [3-eliminated and/or endo H-treated killer toxin preparations probed with polyclonal a-toxin antibodies revealed that the carbohydrate moiety of K28 consists of D-mannose only, which is O-glycosidically linked via Ser/Thr residues to the protein part. The change in gel mobility of K2s after [3-elimination was caused by a decrease in molecular mass of about 1,800, corresponding to a carbohydrate moiety of 10 mannose residues per killer toxin molecule.