Abstract—
The ribosome preparation of goat cerebral cortex was found to possess acid and alkaline phosphodiesterase (PDase) activities, the alkaline PDase activity was greater. The alkaline PDase activity increased sharply between pH 8 and 9 and showed maximum activity between 35° and 40°. The alkaline PDase lost about half of its activity on heating the ribosome preparation at 83° for 5 min. Storage at low temperature or freezing and thawing did not cause significant loss of enzymic activity, but prolonged dialysis beyond 24 hr in the cold against magnesium‐cacodylate buffer caused some loss of activity. Copper, cobalt, inorganic phosphate ions, EDTA, urea and detergents were found to be inhibitors of the PDase activity. Differential inactivation in the presence of arsenate and zinc ions suggests the distinctness of the PDase activity from the phosphomonoesterase (PMase) activity of the ribosome preparation. The enzyme appeared firmly bound to ribosomal particles and attempts to solubilize it were unsuccessful.