Abstract
Glutamic acid decarboxylase was more abundant near the surface than in the center of radish hypocotyls and was accumulated in mature and senescent leaves. There was essentially no effect of B deficiency on enzyme activity. Squash decarboxylase in water solution was partially purified by lyophilization, freezing in solution, precipitation in cold acetone, ammonium sulfate precipitation, or by combinations of these. The enzyme was irreversibly inactivated at pH s outside the range 5.7 - 6.2 and at temperatures above about 54[degree]C. The enzyme lost coenzyme easily during processing or by dialysis but was reactivated with synthetic pyridoxal phosphate.