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. 1988 Feb 29;229(1):21-4.
doi: 10.1016/0014-5793(88)80789-0.

A monoclonal antibody to C1q which appears to interact with C1r2C1s2-binding site

L Hsiung  1 , A W Dodds, D W Mason, K B Reid
Affiliations
Free article

A monoclonal antibody to C1q which appears to interact with C1r2C1s2-binding site

L Hsiung et al. FEBS Lett. .
Free article

Abstract

A monoclonal antibody (SB-4) to human C1q was prepared. The equilibrium constant of the antibody for C1q was found to be greater than 10(10) M-1. It has been shown that the antibody binds to the A-B chain dimer, probably via the B chain of C1q. Pepsin digestion of C1q at pH 4.5, which fragments the globular regions but leaves the collagenous region intact, allowed the demonstration that the antigenic site is located in the collagenous region of the molecule. The effect of the antibody on haemolytic activity has shown that it is capable of inhibiting the formation of EAC1 cells from EAC1q cells plus C1r and C1s but is incapable of inhibiting the C1 activity of performed EAC1 cells. This indicates that the binding of the antibody to the collagenous portion of the B chain of C1q probably prevents interaction between C1q and the C1r2-C1s2 complex.

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