Study of the interaction between monoclonal IgM proteins and the complement system

George Füst, Mária Csécsi-Nagy, George A. Medgyesi, Judit Kulics, János Gergely

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Abstract

The capacity to activate the complement system and to fix isolated C1 of different monoclonal IgM proteins and various fragments was studied. All the 8 different IgM proteins tested fixed isolated C1, but the dose of the IgM preparations necessary for the fixation of the 50% of the available C1 activity strongly differed from each other. The complement activating (anti-complementary) effect of the IgM preparations was weak. (Fcμ)5 fragments prepared by tryptic digestion from 4 different IgM proteins and separated by gel filtration at pH 8.0 could fix C1 and their anti-complementary effect significantly increased with respect to the original IgM preparations. It was demonstrated that the C1-fixing ability of the (Fcμ)5 fragment was lost after gel filtration at pH 3.0 and a C1-fixing low mol. wt peptide fraction was released from the (Fcμ)5. This peptide recombined with the non-C1-fixing (Fcμ)5 and restored its ability for the C1-fixation. It was shown, furthermore, that the (Fcμ)5 preparation which could not fix isolated C1, activated the complement system via the alternative pathway.

Original languageEnglish
Pages (from-to)793-800
Number of pages8
JournalImmunochemistry
Volume13
Issue number10
DOIs
Publication statusPublished - Oct 1976

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ASJC Scopus subject areas

  • Medicine(all)

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