A study of activation levels and transphosphorylase activities associated with the alkaline phosphatase of C57BL mice, 1974

Prioleau, John Clemeau

1970-1979

Levels of activation and transphosphorylation have been studied using crude preparations of alkaline phosphatase (APase). Tris (Hydroxymethyl) aminomethane, Ammediol (2 Amino-2-methy1 1,3 propandiol) and Borate buffers were employed to buffer the reactions. Para-nitrophenyl phosphate was used as the substrate to assay for APase activity. The concentrations of both the hydrolyzed products, para-nitro-phenol and phosphate were measured colorimetrically at appropriate wavelengths. Evidence is presented showing that transphosphorylation is possible at certain concentrations of Tris and Ammediol. An enhanced activation level was also noted with these two nucleophilic buffers. Borate, however, showed no significant activation of APase either at high or low concentrations and little or no transferase activity was detected. Essentially, no significant differences have been shown among the tissue APases of lymphoma, embryo, and placenta with respect to their activation levels.

text

application/pdf

1974-12-01

thesis

Master of Science (MS)

Atlanta University

Biology

Lumb, Judith Rae

Clark Atlanta University

Georgia--Atlanta

http://hdl.handle.net/20.500.12322/cau.td:1974_prioleau_john_c