Stimulation by ATP of alkaline phosphatase in placental plasma membranes.
Biochim Biophys Acta, 1975/5/23;391(1):61-6.
PMID: 166682
Abstract
1. ATP stimulated the p-nitrophenyl phosphatase activity of placental plasma membranes, with an increase in activity of approximately 100% at 5 mM ATP. The stimulation was not dependent on the presence of Mg-2-+. 2. The K-m for p-nitrophenyl phosphate was not changed by the presence of 5 mM ATP. 3. ATP hydrolysis by the plasma membrane preparation under the same assay conditions as for alkaline phosphatase was not influenced by the presence of 5 mM p-nitrophenyl phosphate. 4. Extraction of the plasma membrane preparation with n-butanol abolished the stimulatory effect of ATP, as well as Ca-2-+-activated ATPase activity.
MeSH terms
4-Nitrophenylphosphatase; Adenosine Triphosphatases; Adenosine Triphosphate; Alkaline Phosphatase; Animals; Butanols; Calcium; Cell Membrane; Enzyme Activation; Female; Guinea Pigs; Kinetics; Placenta; Pregnancy
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