Abstract
The binding of three sets of compounds, analogs of phosphorylcholine, to the murine IgA myeloma proteins McPC 603, MOPC 167 and S107 has been studied by the method of hapten inhibition of precipitation. The three sites were of the general formulae (CH 3) 3N +(CH 2( n COOH, (CH 3) 3N +(CH 2) n CH 2OH and (CH 3) 3N +(CH 2) n Ph. All three proteins showed similar behavior with the carboxylate compounds, maximum activity occurring at n=3, the closest analog of phosphorylcholine. In contrast, the phenyl and alcohol series behaved in a different fashion with each protein. In the case of S107 the phenyl compounds were almost as effective as the carboxylate ones. Only MOPC 267 showed strong binding of the hydroxyl compounds. Thus, despite their structural similarities and common reactivity to the phosphorylcholine determinant the three proteins show significantly different reactivities towards related compounds.
Published Version
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