Date of Award


Degree Type


Degree Name



Department of Biology

First Advisor

Dr. Judith Rae Lumb


Alkaline phosphatase (APase), normally found in lymphocytes up to sixteen days gestation in C57B1 mice, has been associated with murine lymphomas. Previous studies of APase activities of lymphoma and normal tissue have shown a specific pyrophosphatase activity and a nonspecific APase activity which hydrolyzes beta-glycerophosphate, alpha-naphthylphosphate and p-nitrophenylphosphate. To establish the function of this APase activity, further biochemical characterizations of this enzyme were studied, using adenosine 5' - triphosphate (AIP) and fructose 1,6-diphosphate (FDP) as substrates. The parameters used were pH optimum, substrate concentration and substrate ratio, heat inactivation, ethylenediamine tetraacetic acid (EDTA) and phenylalanine inhibitions, and magnesium activation. The results show no significant differences in placental and lymphoma AlPase and FDPase activities with respect to pH optimum, phenylalanine inhibition, substrate ratios and heat inactivation rate. However, substrate ratios show additional ATPase activity in the normal adult spleen. ATPase and FDPase activities appear to be different by EDTA inhibition and magnesium activation. However, this may reflect differences in active substrate rather than different enzymes. In comparison to the nonspecific APase activity previously described, ATPase and FDPase show a greater rate of heat inactivation. However, the biphasic nature of the inactivation patterns, with the exception of lymphoma FDPase, may indicate the presence of other enzymes which show affinity to these substrates. The present data do not conclusively rule out the possibility that nonspecific APase activity may demonstrate dephosphorylation of ATP and FDP. Further elucidation of this relationship must await purification of this enzyme.