Literature DB >> 1417879

Interaction of Artocarpus lectins with human IgA does not involve asparagine-linked oligosaccharide of the immunoglobulin.

O H Hashim1, K Kobayashi, N Taniguchi.   

Abstract

In view of the controversy with respect to the interaction of jacalin with human IgA2, a study was undertaken to assess the reactivity of the Artocarpus heterophyllus lectin, as well as the lectin from Artocarpus integer (lectin C), with subclasses of human immunoglobulin A by ELISA. Our data is consistent with the view that Artocarpus lectins have no affinity for the IgA2 immunoglobulins. In further support of the findings, we have established that N-linked oligosaccharide moieties of IgA have no significant bearing in the lectin-immunoglobulin binding. Interaction was also not affected in the presence of 1% (w/v) BSA.

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Year:  1992        PMID: 1417879

Source DB:  PubMed          Journal:  Biochem Int        ISSN: 0158-5231


  2 in total

1.  Aberrant glycosylation of IgA from patients with IgA nephropathy.

Authors:  D Baharaki; M Dueymes; R Perrichot; C Basset; R Le Corre; J Clèdes; P Youinou
Journal:  Glycoconj J       Date:  1996-08       Impact factor: 2.916

2.  Agaricus bisporus lectin binds mainly O-glycans but also N-glycans of human IgA subclasses.

Authors:  F J Irazoqui; F E Zalazar; G A Nores; M A Vides
Journal:  Glycoconj J       Date:  1997-04       Impact factor: 2.916

  2 in total

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