Isolation of a mannose-binding and IgE- and IgM-reactive lectin from the seeds of Artocarpus integer
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 co...
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| Main Authors: | , , |
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| Format: | Article |
| Language: | en |
| Published: |
1997
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| Subjects: | |
| Online Access: | http://eprints.um.edu.my/3448/1/Isolation_of_a_mannose-binding_and_IgE-_and_IgM-reactive_lectin.pdf http://eprints.um.edu.my/3448/ http://www.sciencedirect.com/science/article/pii/S0022175997001580 |
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| Summary: | 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. |
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