Multiple forms of acid phosphatase in rat secretory enamel organ.

Acid phosphatase activity was studied biochemically in homogenates of secretory enamel organs from the rat. Incubations with crude homogenate failed to show distinct pH optima or kinetics characteristic for single enzymes. Crude homogenate activity was strongly inhibited by concentrations higher than 1 mM of NaF and Na-tartrate, and higher than 10 mM of ZnSO4 and para-bromotetramisole oxalate. 10 mM MgCl2 gave a slight stimulation. CaCl2, KCl and EDTA were uneffective. Electrophoretic separation of the crude homogenate acid phosphatase on Triton X-100 containing polyacrylamide gel demonstrated the presence of at least three multiple forms of the enzyme. Two of them showed distinct pH optima at pH 4.4. The third one showed a broad pH plateau in the acid pH range. Kinetic studies of the three forms indicated single enzyme reactions. Two forms had electrophoretic mobilities similar to alkaline phosphatase. One form could be solubilized only after Triton X-100 treatment. All forms were strongly sensitive to 10 mM NaF when added to the reaction mixture. The sensibility to 10 mM ZnSO4, CuSO4, Na-tartrate and para-bromotetramisole oxalate differed between the different forms.