The application of Artocarpus integer seed lectin-M in the detection and isolation of selective human serum acute-phase proteins and immunoglobulins
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-...
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| Main Authors: | , , |
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| Format: | Article |
| Published: |
2001
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| Subjects: | |
| Online Access: | http://eprints.um.edu.my/3445/ http://informahealthcare.com/doi/abs/10.1081/IMM-100104021 |
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| Summary: | 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. |
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