Hashim, Onn Haji and Ahmad, F. and Shuib, A.S. (2001) The application of Artocarpus integer seed lectin-M in the detection and isolation of selective human serum acute-phase proteins and immunoglobulins. Immunological Investigations, 30 (2). pp. 131-141. ISSN 0882-0139, DOI https://doi.org/10.1081/imm-100104021.
Full text not available from this repository.Abstract
Champedak (Artocarpus integer) lectin-M is a lectin with high specificity and affinity for the core-mannosyl residues of the N-linked oligosaccharides of glycoproteins. We have studied the interaction of the champedak seed lectin with human serum glycoproteins that were resolved by 2-dimensional (2-D) gel electrophoresis. The lectin demonstrated strong interaction with haptoglobin beta chain, orosomucoid, al-antitrypsin, alpha (2)-HS glycoprotein, transferrin, hemopexin, alpha B-1-glycoprotein, and the heavy chains of IgA, IgM and IgG of the human serum. With exceptions of the heavy chains of the immunoglobulins and alpha B-1-glycoprotein, all the other lectin-M-probed glycopeptides are acute-phase proteins. The use of champedak lectin-h l to probe for serum glycoproteins that were separated in a 2-D gel electrophoresis and Western blotting technique may be conveniently applied to analyse the acute-phase and humoral immune responses simultaneously. Subjecting human serum to immobilised-lectin-M affinity chromatography was able to isolate intact haptoglobin, alpha (1)-antitrypsin, alpha B-1-glycoprotein, hemopexin and IgA.
Item Type: | Article |
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Funders: | UNSPECIFIED |
Additional Information: | Department of Molecular Medicine, Faculty of Medicine Building, University of Malaya, 50603 Kuala Lumpur, MALAYSIA ---> Hashim, OH Ahmad, F Shuib, AS |
Uncontrolled Keywords: | Molecular Medicine |
Subjects: | R Medicine |
Divisions: | Faculty of Medicine |
Depositing User: | Ms Haslinda Lahuddin |
Date Deposited: | 11 Jul 2012 01:32 |
Last Modified: | 24 Oct 2019 08:20 |
URI: | http://eprints.um.edu.my/id/eprint/3445 |
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