Date of Award
Department of Biology
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.
Njoku, Oliver O., "Biochemical comparison of n-alkaline phosphatase with other alkaline phosphatases in normal and leukemic tissues of c57bl mice" (1981). ETD Collection for AUC Robert W. Woodruff Library. 3831.