Abstract:
:To investigate the effect of carbohydrate on activation of the alternative pathway of complement by IgA immune complexes, aglycosylated monoclonal IgA was made biosynthetically in the presence of tunicamycin. When immune complexes were incubated with normal human serum (NHS), the aglycosylated IgA immune complexes caused less depletion of the alternative pathway activity of the serum. They also bound less C3 and produced less terminal complement complexes. The binding of C3 to both immune complexes was mainly through hydroxylamine sensitive ester bonds. C3 did not bind to free IgA.
journal_name
Immunologyjournal_title
Immunologyauthors
Zhang W,Lachmann PJsubject
Has Abstractpub_date
1994-01-01 00:00:00pages
137-41issue
1eissn
0019-2805issn
1365-2567journal_volume
81pub_type
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