Interaction of antimannan with glycopeptides |
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Authors: | Nobuyuki Itoh Ikuo Yamashina |
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Institution: | Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, Kyoto 606, Japan |
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Abstract: | Taka amylase A glycopeptide (TA-GP) strongly inhibited the interaction of antimannan (antibodies directed towards mannan from ) with yeast mannan, whereas ovalbumin glycopeptide (OA-GP) did so only poorly. We inferred that this is due to the strong reactivity of antimannan with terminal trimannosides composed of Manα1→2Man or Manα1→3Man linkages which occur in mannan and TA-GP. In contrast, TA-GP and OA-GP were nearly equally reactive with concanavalin A having the ability to interact with terminal mannose and 2-0-mannose residues which occur abundantly in these glycopeptides. Thus, antimannan should be useful as a probe for characterizing glycoproteins from extracellular fluids or cellular membranes. |
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