Abstract
Alkaline inorganic pyrophosphatase from Zea mays removed pyrophosphate inhibition of RNA synthesis, on addition to E. coli RNA polymerase directed by chromatin from etiolated Glycine max. The ionic environment of the coupled reactions, even when optimized, caused reduced efficiency of both enzymes. Competition for Mg 2+ by alkaline pyrophosphatase reduced RNA polymerase activity in vitro. The Mn 2+ concentration optimal for RNA polymerase decreased the activity of alkaline inorganic pyrophosphatase by 80 per cent.
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