Immunochemical analysis of the carbohydrate moiety of yeast killer toxin K28 |
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Authors: | Manfred J Schmitt Peter C Pfeiffer |
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Institution: | (1) Institut für Mikrobiologie und Weinforschung der Johannes Gutenberg, Universität Mainz, Postfach 3980, D-6500 Mainz, Germany |
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Abstract: | 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 -eliminated and/or endo H-treated killer toxin preparations probed with polyclonal -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 -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. |
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Keywords: | Saccharomyces cerevisiae killer toxin K28 glycoprotein O-glycosylation -elimination" target="_blank">gif" alt="beta" align="MIDDLE" BORDER="0">-elimination -toxin antibodies" target="_blank">gif" alt="agr" align="BASELINE" BORDER="0">-toxin antibodies |
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