The phosphatase activity of spleen extracts

Abstract

The phosphatase activity with varying pH values, of extracts of bullock, calf, sheep and dog spleens showed two optima, one at pH 4.5-5.0 (the "acid" enzyme) and the other at pH 9.0 (the "alkaline" enzyme, possibly identical with the bone enzyme of Robison). The ratio of activity of the "acid" and "alkaline" enzymes of the spleen, at their two optima was not constant either from sp. to sp. or from animal to animal in the same species. The greatest activating effect of Mg ions on the spleen enzymes occurred at pH values near neutrality. The "acid" enzyme hydrolyzed Na [beta] glycerophosphate much faster (ca. 300%) than the corresponding a iso-meride. This is contrary to the behaviour of the red cell enzyme.