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

Lim, S.B. and Chua, C.T. and Hashim, Onn Haji (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, DOI https://doi.org/10.1016/s0022-1759(97)00158-0.

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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
Funders:	UNSPECIFIED
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 01:40
Last Modified:	24 Oct 2019 08:15
URI:	http://eprints.um.edu.my/id/eprint/3448

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