Biochemical comparison of n-alkaline phosphatase with other alkaline phosphatases in normal and leukemic tissues of c57bl mice, 1981
Njoku, Oliver O.
1980-1989
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.
text
application/pdf
1981-07-01
thesis
Master of Science (MS)
Atlanta University
Department of Biology
Lumb, Judith Rae,
Clark Atlanta University
Georgia--Atlanta
http://hdl.handle.net/20.500.12322/cau.td:1981_njoku_oliver_o