Date of Award


Degree Type


Degree Name



Department of Biology

First Advisor

Dr. Judith Rae Lumb


In order to compare the catalytic properties of alkaline phosphatases (APases) in various tissues, two types of monophosphate esters, p-nitrophenyl phosphate (pNPP) and cysteamine-S-phosphate (CASP), were chosen. Alkaline phosphate activity in different tissues of C57BL mice, both normal and leukemic, has been demonstrated to hydrolyze both p-nitrophenyl phosphate and cysteamine-S-phosphate. However, the rate of hydrolysis of p-nitrophenyl phosphate was greater than that of cysteamine-S-phosphate. Higher activity was observed in pH 10.0 than pH 9.0 in both Tris-HCL and diethanolamine buffers used. Diethanolamine buffer activated the APase activities more than Tris-HCL buffer. There was no significant difference between the APases of the spleen, whole embryo, thymic lymphoma and placenta, based on the rate of hydrolysis of p-nitrophenyl phosphate to the rate of the hydrolysis of cysteamine-S-phosphate. It is concluded on the basis of this study that thymic lymphoma APase, like other APases of C57BL mice, has higher affinity for pNPP than CASP.