The reactivity of mononucleotides with cholecystokinin/gastrin antisera.
Dibutyryl cyclic GMP has been reported to interact with antisera specific for C-terminal tetrapeptide amide common for cholecystokinin (CCK) and gastrin. Moreover, cyclic nucleotides elute by gel chromatography in the same position as the free CCK/gastrin tetrapeptide. Therefore, we have examined the reactivity of 25 mononucleotides with eight CCK and gastrin antisera. The results show that the nucleotides all bind poorly to the antisera (nucleotide concentration required greater than 1 mM). Hence, endogenous cyclic nucleotides, which are present in biological extracts in pM to nM concentrations, do not interfere with immunochemical CCK or gastrin measurements. The antisera displayed highly individual patterns of reactivity without preferential binding of di- or monobutyryl cyclic nucleotides (AMP, GMP or IMP). Thus, the present results do not support the idea of structural resemblance between the C-terminus of CCK/gastrin peptides and butyryl derivatives of cyclic GMP. Enzymatic treatment of the antral tetrapeptide-like immunoreactivity showed that nucleotides do not contribute to this material, which appears exclusively peptidergic.
D000818:Animals; D002766:Cholecystokinin / Q000276:immunology*; D005755:Gastrins / Q000276:immunology*; D006728:Hormones / Q000276:immunology*; D006801:Humans; D007106:Immune Sera; D010446:Peptide Fragments / Q000276:immunology*; D011863:Radioimmunoassay; D012265:Ribonucleotides; D013329:Structure-Activity Relationship; D013552:Swine
D005755:Gastrins; D006728:Hormones; D007106:Immune Sera; D010446:Peptide Fragments; D012265:Ribonucleotides; C013550:gastrin 17; D002766:Cholecystokinin