PhosphorylaseaActivity in Rat Uterine Homogenates: Protection by Ethylenediaminetetraacetate

Abstract
The chelating agent, EDTA prevented time-dependent decreases in phosphorylase a activity during assay. Total phosphorylase t activity estimated in the presence of adenosine-5''-monophosphate (AMP) did not change. EDTA appears to prevent conversion of active rat uterine phosphorylase a to a form which requires AMP for catalytic activity.