Cytidine-5'-diphospho-choline conjugates. I.--Synthesis and fixation to phosphorylcholine-binding proteins

The oxidation of the ribose ring of cytidine-5'-diphospho-choline (CDPC) by periodate to produce reactive dialdehydes was used to couple this activated reagent onto various proteins, onto Ficoll 400 and onto Sepharose 4B. Careful control of parameters of the different steps of the reaction enabled us to synthesize conjugates with a graded number of nucleotide residues. Human serum albumin conjugates with a relatively high degree of substitution were used to demonstrate and to measure anti-phosphorylcholine antibodies and the acute phase reactant, C-reactive protein by precipitation or passive haemagglutination techniques. These methods for measuring C-reactive protein in serum of patient suffering from acute inflammation may be useful for clinicians. CDPC-AH Sepharose was used to purify the phosphorylcholine-binding myeloma protein HOPC8 and to separate C-reactive protein from the bulk of serum proteins. Improvements of this technique will certainly lead to the complete purification of C-reactive protein.