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Human Placental Alkaline Phosphatase And Steroid Metabolism By Rat Adrenals, Allen G. Meier
Human Placental Alkaline Phosphatase And Steroid Metabolism By Rat Adrenals, Allen G. Meier
Loma Linda University Electronic Theses, Dissertations & Projects
Human placental alkaline phosphatase was purified by butanol extraction, methanol precipitation and chromatography on DEAE-cellulose. The pH optimum was found to be 10.9. The enzyme was competitively inhibited by di-ethyl-p-nitrobenzyl-phosphonate and copper sulfate. An increase in enzymatic activity occurred in the presence of the phosphate ion (HPO4) and ATP.
The enzyme was crystallized from a 40% saturated solution of ammonium sulfate and shown to be homogeneous by sedimentation analysis. Homogeneity of the enzyme was also demonstrated using poly-acrylamide-gel-electrophoresis. At a pH of 7.5% the electrophoretic pattern yielded a single band and showed no significant contamination.
The metabolic transformation …