Abstract

Fractionation of extracts from prostaglandin E 1-treated cells by polyacrylamide gel electrophoresis followed by subsequent assay of the gel slices for cyclic AMP-and cyclic GMP phosphodiesterase activities reveals multiple activities, which differ from the activities demonstrable in controls, upon assay with low levels of substrate. Preparation of extracts by gentle homogenization under isotonic conditions show the absence of some cyclic AMP phosphodiesterase activities otherwise detectable in the super-natants of hormone-treated cell extracts obtained by freezing and thawing. No such adherence to particulate fractions is obvious in comparable extracts from control cells.

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