Abstract
Rabbit gamma globulin anti-adenosine monophosphate-egg albumin (AMP-EA) was used to study the molecular conformation of nucleotides such as adenosine triphosphate (ATP) or adenosine diphosphate (ADP). The study was done uisng AMP, ADP, and ATP, under different conditions, to inhibit the precipitin reaction between AMP-human serum albumin (HSA) and anti-AMP-EA. When the haptens were dissolved in 0·15 M saline at pH 7·0, the best inhibitor was AMP followed by ADP and then by ATP. If the haptens were dissolved in 0.02 M disodium ethylene diamino tetra-acetate (EDTA)-0.15· M saline at pH 7·0, the inhibition by AMP was not modified but both ADP and ATP inhibited as well as AMP. Finally if the haptens were dissolved in 0·02 M MgCl 2 -0·15 M saline at pH 7·0, again AMP inhibited as before but ADP and ATP inhibited less than wehn dissolved in saline alone. ATP in saline or with magnesium ions (Mg ++ ) inhibited less than ADP in the same conditions. These results indicate that ADP and ATP have a folded molecular conformation with Mg ++ participating in it in such a way that antibodies specific for the adenine base cannot react with them as well as with AMP which does not have this folded configuration. EDTA removes the Mg ++ , causing an unfolding of the ATP or ADP molecule and facilitating in this way their reaction with anti-AMP antibodies in the same manner as with AMP alone.
Published Version
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