Immunochemical analysis of the carbohydrate moiety of yeast killer toxin K28.
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 beta-eliminated and/or endo H-treated killer toxin preparations probed with polyclonal alpha-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 K28 after beta-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.
Schmitt
M J
MJ
Institut für Mikrobiologie und Weinforschung, Johannes Gutenberg-Universität Mainz, Germany.
Pfeiffer
P C
PC
D000908:Antibodies, Fungal / Q000096:biosynthesis; D015153:Blotting, Western; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D006031:Glycosylation; D007120:Immunochemistry; D055646:Killer Factors, Yeast; D008358:Mannose / Q000032:analysis; D009183:Mycotoxins / Q000737:chemistry* / Q000276:immunology; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000276:immunology; D029701:Saccharomyces cerevisiae Proteins; D012685:Sepharose / Q000031:analogs & derivatives
D000908:Antibodies, Fungal; D055646:Killer Factors, Yeast; D009183:Mycotoxins; D029701:Saccharomyces cerevisiae Proteins; C028326:concanavalin A-sepharose; D012685:Sepharose; D008358:Mannose