Floyd, Rachael A

Description

Degree Name: Doctor of Philosophy (PhD)Date of Degree: 1976Granting Institution: Atlanta UniversityDepartment/ School: Department of BiologyAlthough the association of alkaline phosphatase (APase) with murine fetal thymus up to 16 days gestation and murine thymic lymphoma has been established, very little work has been done to determine if the murine lymphoma APase is similar to the fetal thymus APase. In an effort to determine the nature of the relationship a biochemical characterization was performed. The placenta and spleen were also included since previous biochemical experiments had shown lymphoma APase similar to these APases. The parameters included pH optimum, heat inactivation, substrate ratios, Michaelis constant, activation and inhibition. In addition, the electrophoretic mobility was determined in the presence and absence of neuraminidase using the substrates alpha-naphthyl phosphate (NP) and p-nitrophenyl phosphate (pNPP). The results indicate that the lymphoma APase is very similar to fetal thymus, placenta, and spleen APases. All APase activities had a pH optimum of 10. Approximately 557, of the activity was inactivated at 55 C in four minutes. The APase activities were all inhibited by ethylenediamine tetra-acetic acid, L-homoarginine, and L-phenylalanine at the level of 100, 80 and 7.717, respectively. Magnesium activated each APase activity by approximately 467. Furthermore, the nucleophilic buffers diethanolamine, 2-amino-2-methy1-1,3-pro- pandiol, and tris(hydroxymethyl)aminomethane activated the APase activities. The electrophoretic mobility of all APases was similar and neuraminidase slowed the migration of these APase activities. The localization of each APase was identical with the substrates NP and pNPP. These results lend support to the hypothesis that...

Record Contributed By

Clark Atlanta University

Record Harvested From

Digital Library of Georgia