抄録
Five clones of mouse monoclonal antibody (mAb) against human C-reactive protein (CRP) were established by the hybridoma technique. Each of these mAbs formed a precipitin line with CRP, showing a spur to the line produced by rabbit polyclonal antiserum against CRP. Five mAbs were divided into two groups: the precipitin lines formed by mAbs in one group fused completely with each other, and those formed by mAbs in the other group formed spurs. Mixtures of the two groups of mAbs produced precipitin lines identical to those produced by the polyclonal antibodies. On the other hand, ethylene glycol-bis (2-aminoethyl ether) tetraacetic acid and phosphorylcholine, which are known to bind with CRP, inhibited the formation of complexes by CRP with the mAbs of one group, but not of the other group. However, N-acethyl-galactosamine, which is also known to bind with CRP, showed no blocking effect on the mAbs of either group. The findings suggest that there are at least two different epitopes on a CRP molecule, each of which is recognized by mAbs of either group. The mAbs might be useful for the clinical assay of serum CRP and for the study of the structure of epitopes of CRP.
