Abstract
1. 1. Alkaline phosphatase from rat osseous plate catalyzed the transfer of phosphate from p-nitrophenylphosphate to glycerol, ethanolamines. Tris, glucose and l-amino-l-methyl-2-propanol, in a wide range of pH. Serine did not stimulate phosphotransferase activity of the enzyme. 2. 2. The best phosphotransferase acceptors were diethanolamine and glycerol while glucose was the poorest phosphotransferase acceptor used. 3. 3. Diethanolamine and glycerol affected both V M and K M of p-nitrophenylphosphate hydrolysis with activation constants ( K A) of 0.25 and 0.85 M, respectively. 4. 4. A kinetic model was proposed for the phosphotransferase reaction observed with alkaline phosphatase from rat osseous plates.
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