Isolation of a mannose-binding and IgE- and IgM-reactive lectin from the seeds of Artocarpus integer

Lim, S.B.; Chua, C.T.; Hashim, O.H. (1997) Isolation of a mannose-binding and IgE- and IgM-reactive lectin from the seeds of Artocarpus integer. Journal of Immunological Methods, 209 (2). pp. 177-186. ISSN 0022-1759

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    Abstract

    A mannose-binding lectin, termed champedak lectin-M, was isolated from an extract of the crude seeds of champedak (Artocarpus integer). On gel filtration chromatography, the lectin eluted in a single peak at elution volumes corresponding to 64 kDa, SDS-PAGE showed the mannose-binding lectin to be composed of 16.8 kDa polypeptides with some of the polypeptides being disulphide-linked to give dimers. When tested with all isotypes of immunoglobulins, champedak lectin-M demonstrated a selective strong interaction with human IgE and IgM, and a weak interaction with IgA2, The binding interactions of lectin-M were metal ion independent. The lectin was also shown to interact with horseradish peroxidase, ovalbumin, porcine thyroglobulin, human alpha(1)-acid glycoprotein, transferrin and alpha(1)-antitrypsin. It demonstrated a binding preference to Man alpha 1-3Man ligands in comparison to Man alpha 1-6Man or Man alpha 1-2Man. (C) 1997 Elsevier Science B.V.

    Item Type: Article
    Creators:
    1. Lim, S.B.
    2. Chua, C.T.
    3. Hashim, O.H.(Department of Molecular Medicine, Faculty of Medicine Building, University of Malaya, 50603 Kuala Lumpur, MALAYSIA)
    Journal or Publication Title: Journal of Immunological Methods
    Additional Information: Correspondence author. Fax: q60-3-7594957; e-mail: onnhashim@medicine.med.um.edu.my
    Uncontrolled Keywords: Lectin; IgE; IgM; Mannose; Artocarpus integer
    Subjects: R Medicine
    Divisions: Faculty of Medicine
    Depositing User: Ms Haslinda Lahuddin
    Date Deposited: 11 Jul 2012 09:40
    Last Modified: 11 Jul 2012 09:40
    URI: http://eprints.um.edu.my/id/eprint/3448

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