ISSN:
1365-3083
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
Lectin selectivity for human ig classes is based on carbohydrate differences. Earlier reports that the lectin jacalin precipitated human igA were confirmed and supplemented by the current study, which demonstrates that jacalin also binds human IgD as evaluated by micro-ELlSA and SDS-PAGE. Experimental findings indicated that: (i) Monoclonal and polyclonal (sera) IgD. IgAl, bul not IgA2, IgM, or IgGI-4 reacted with jacalin, (ii) Six tested monoclonal IgD proteins each bound approximately equally to jacalin when antigenicity rather than protein concentration was measured; the results weigh against the presence of jacalin-delectable IgD subclasses or genetic variants, (iii) IgD and IgAl both associated maximally in 4-8h at 4°C. There was no dissociation at 4°C but limited dissociation occurred at 37°C after 24h, (iv) Both IgD and IgAl were eluted from jacalin by galaetose-related sugars, (v) IgD and IgAI bind competitively to jacalin. The results suggested that jacalin reacts with O-linkcd oligosaccharide N-acetyl-galactosamine (GalN) residues found on the hinge region of both IgD and IgAl, Jacatin also interacted with one major and several minor unidentified sera proteins. The findings offer an approach to the isolation of serum polyclonal IgD and to the characterization of the unusual carbohydrates of the human delta heavy chain with respect to their function.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-3083.1987.tb02256.x
