The interaction of selective plant lectins with neuraminidase-treated and untreated IgA1 from the sera of IgA nephropathy patients

A study on the binding interaction of lectins from Artocarpus heterophyllus (jacalin), Glycine max and Sambucus nigra with standardised quantity of IgA from the IgA nephropathy patients and normal controls was performed. The Glycine max lectin demonstrated higher affinity towards the serum IgA of Ig...

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Main Authors: Hashim, Onn Haji, Shuib, A.S., Chua, C.T.
Format: Article
Published: 2001
Subjects:
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author Hashim, Onn Haji
Shuib, A.S.
Chua, C.T.
author_facet Hashim, Onn Haji
Shuib, A.S.
Chua, C.T.
author_sort Hashim, Onn Haji
collection UM
description A study on the binding interaction of lectins from Artocarpus heterophyllus (jacalin), Glycine max and Sambucus nigra with standardised quantity of IgA from the IgA nephropathy patients and normal controls was performed. The Glycine max lectin demonstrated higher affinity towards the serum IgA of IgAN patients as compared to normal controls. However, the affinity binding was lower in cases of jacalin and the Sambucus nigra lectin. When serum samples were treated with neuraminidase, the differential jacalin affinity binding between IgA1 of patients and normal controls was abrogated. Our data are in support of the view that the O-linked oligosaccharide moieties of the patients IgA1 were generally lacking in galactose and sialic acid residues.
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spelling um.eprints-34432019-10-24T08:20:18Z http://eprints.um.edu.my/3443/ The interaction of selective plant lectins with neuraminidase-treated and untreated IgA1 from the sera of IgA nephropathy patients Hashim, Onn Haji Shuib, A.S. Chua, C.T. R Medicine A study on the binding interaction of lectins from Artocarpus heterophyllus (jacalin), Glycine max and Sambucus nigra with standardised quantity of IgA from the IgA nephropathy patients and normal controls was performed. The Glycine max lectin demonstrated higher affinity towards the serum IgA of IgAN patients as compared to normal controls. However, the affinity binding was lower in cases of jacalin and the Sambucus nigra lectin. When serum samples were treated with neuraminidase, the differential jacalin affinity binding between IgA1 of patients and normal controls was abrogated. Our data are in support of the view that the O-linked oligosaccharide moieties of the patients IgA1 were generally lacking in galactose and sialic acid residues. 2001 Article PeerReviewed Hashim, Onn Haji and Shuib, A.S. and Chua, C.T. (2001) The interaction of selective plant lectins with neuraminidase-treated and untreated IgA1 from the sera of IgA nephropathy patients. Immunological Investigations, 30 (1). pp. 21-31. ISSN 0882-0139, DOI https://doi.org/10.1081/imm-100103688 <https://doi.org/10.1081/imm-100103688>. http://www.ncbi.nlm.nih.gov/pubmed/11419909 10.1081/imm-100103688
spellingShingle R Medicine
Hashim, Onn Haji
Shuib, A.S.
Chua, C.T.
The interaction of selective plant lectins with neuraminidase-treated and untreated IgA1 from the sera of IgA nephropathy patients
title The interaction of selective plant lectins with neuraminidase-treated and untreated IgA1 from the sera of IgA nephropathy patients
title_full The interaction of selective plant lectins with neuraminidase-treated and untreated IgA1 from the sera of IgA nephropathy patients
title_fullStr The interaction of selective plant lectins with neuraminidase-treated and untreated IgA1 from the sera of IgA nephropathy patients
title_full_unstemmed The interaction of selective plant lectins with neuraminidase-treated and untreated IgA1 from the sera of IgA nephropathy patients
title_short The interaction of selective plant lectins with neuraminidase-treated and untreated IgA1 from the sera of IgA nephropathy patients
title_sort interaction of selective plant lectins with neuraminidase treated and untreated iga1 from the sera of iga nephropathy patients
topic R Medicine
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