Abstract
Thirteen mouse hybridomas secreting monoclonal antibodies (MAbs) to human C-reactive protein (CRP) were generated and characterized. The relative avidity of the MAbs for CRP ranged from 0.005 to 8.6 micrograms/ml of purified Ig. Several of the MAbs recognized an epitope on CRP expressed only in the presence of physiological levels of Ca++. The epitope specificity of the 13 MAbs was examined by testing their cross-reactivity and allowed us to assign them to two groups. Group I MAbs recognized the Ca++-dependent phosphorylcholine (PC)-binding site of CRP since their reactivity was inhibited by PC. Group II MAbs recognized epitopes not affected by binding of PC by CRP. The results suggest that these MAbs may be suitable for assigning functional properties of CRP to specific peptide sequences.
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