Acid phosphatase localization in rabbit eosinophils.

Eosinophil (and heterophil) leukocytes of glycogen-induced rabbit peritoneal exudates were fixed for 1(1/2) min in 2% glutaraldehyde and examined for acid phosphatase activity both biochemically and cytochemically. Biochemical assays showed that enzymatic activity had been inhibited by only approximately 10% under these conditions. The cytochemical reaction in the eosinophil was confined to the granules in which the reaction product appeared in the matrix, not in the crystalline core (or in the core region after the latter's extraction). Granules wherein the matrix was disrupted and the crystalline core degraded or extracted showed the most intense deposition of reaction product, whereas well preserved granules with morphologically intact matrix and crystals were unreactive. Yet, not all disrupted granules gave a positive reaction, indicating that disruption was a necessary but not sufficient condition for reactivity. In many eosinophil leukocytes, most if not all granules were acid phosphatase-positive, provided they had become disrupted to a certain degree. Factors possibly involved in converting the granules from an unreactive to a reactive state are discussed.