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C1q binding by a high affinity anti-fluorescein murine monoclonal IgM antibody and monomeric subunits.

Abstract：

:Comparative interactions of purified rabbit C1q with 18-2-3, a high affinity (2-3 X 10(10) M-1) anti-fluorescein (anti-F1) murine monoclonal IgM antibody (pentamer) and constitutive monomeric subunits (IgMs) were studied. Using a solid phase radioimmunoassay (SPRIA), based on immobilized polyvalent antigen, it was shown that the mechanism of C1q binding to IgM was characteristically multiphasic while IgMs yielded monophasic binding curves. The latter compared qualitatively and quantitatively with a monoclonal IgG2a anti-fluorescein antibody with the same intrinsic affinity of 2-3 X 10(10) M-1. C1q binding efficiency to antibodies was significantly enhanced when the immunoglobulins interacted with immobilized multivalent antigen. Monoclonal IgM antibody bind identically to six F1-carrier protein conjugates independent of epitope (F1) density. In contrast, the C1q-antibody interaction binding was dependent upon epitope density. An average distance between F1 epitopes of 80 A was optimal for C1q binding by IgM. At low concn of IgM, when fluorescein was bound by antigen-binding sites on adjacent subunits of an intact pentamer, C1q appeared to bind IgM intramolecularly.

journal_name

Mol Immunol

journal_title

Molecular immunology

authors

Swanson SM,Dombrink-Kurtzman MA,Voss EW Jr

doi

10.1016/0161-5890(88)90076-4

subject

Has Abstract

pub_date

1988-06-01 00:00:00

pages

545-54

issue

6

eissn

0161-5890

issn

1872-9142

journal_volume

25

pub_type

杂志文章

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