Abstract

1. 1. The subcellular distributions of adenyl cyclase and phosphodiesterase were determined in Acanthamoeba palestinensis. The cells were homogenized and fractionated by a technique modified to preserve enzyme activity and monitored by electron microscopy. 2. 2. The recovery of adenyl cyclase activity was highest in the microsomal fraction. Upon further fractionation of the microsomes, adenyl cyclase was concentrated by the rough endoplasmic reticulum fraction, and in only this fraction was the specific activity of the enzyme increased over the starting material. 3. 3. The specific activity of adenyl cyclase was lower in enriched fractions of plasma membranes and mitochondria than in the homogenate, and the recoveries were very low. Further, these fractions revealed the presence of sufficient rough endoplasmic reticulum contamination to account for the adenyl cyclase activity present. 4. 4. Most of the phosphodiesterase activity was soluble and was recovered in the post-microsomal supernatant.

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