CORONARY DILATOR ACTION OF THE ADENINE-ATP SERIES

¹ Division of Biological Research, G. D. Searle & Co., Chicago 80, Illinois

The relative coronary dilator activity of the adenine-ATP series was determined by the intracoronary route in anesthetized open chest dogs. Molar potency values were as follows: ATP 100, ADP 95, muscle AMP 28, adenosine 25 and adenine inactive. Yeast AMP has about one-third the activity of muscle AMP. Ribose, ribose phosphate, sodium orthophosphate and sodium pyrophosphate were inactive. Mixtures of these with adenine, adenosine or AMP to simulate adenosine, AMP, ADP or ATP were no more active than the original substances. Creatine phosphate did not produce dilatation.

The basic requirement for the coronary dilator activity of this series is the adenine-9-riboside moiety. The phosphate in muscle AMP does not change the action. However, the second phosphate, as in ADP, greatly enhanced the activity; a third phosphate, as in ATP, had no further effect. It could not be determined whether or not the enhancement of the dilator action was associated with energy of the pyrophosphate bonds in ADP or ATP.

This article has been cited by other articles:

				D. J. Cheek, J. M. McHugh, J. Blood-Siegfried, J. F. McFetridge, and B. S. Turner A Historical Perspective on the Discovery of Adenyl Purines Biol Res Nurs, April 1, 2000; 1(4): 265 - 275. [Abstract] [PDF]