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, alpha1-antitrypsin, alpha2-HS glycoprotein, transferrin, hemopexin, alpha1B-glycoprotein, and the heavy chains of IgA, IgM and IgG of the human serum. With exceptions of the heavy chains of the immunoglobulins and alpha1B-glycoprotein, all the other lectin-M-probed glycopeptides are acute-phase proteins. The use of champedak lectin-M 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, alpha1-antitrypsin, alpha1B-glycoprotein, hemopexin and IgA.
journal_name
Immunol Investjournal_title
Immunological investigationsauthors
Hashim OH,Ahmad F,Shuib ASdoi
10.1081/imm-100104021subject
Has Abstractpub_date
2001-05-01 00:00:00pages
131-41issue
2eissn
0882-0139issn
1532-4311journal_volume
30pub_type
杂志文章abstract:BACKGROUND:Mouse experimental autoimmune encephalomyelitis (EAE) is widely used model of multiple sclerosis (MS). The role of autoreactive CD4+ and CD8+ T cells in the development of mouse EAE has been demonstrated. However, little information is available about the relation between the frequency and reactivity of myel...
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journal_title:Immunological investigations
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