Publication: ALLOSTERIC MODULATION BY ATP, CALCIUM AND MAGNESIUM-IONS OF RAT OSSEOUS PLATE ALKALINE-PHOSPHATASE
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Graduate program
Undergraduate course
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Publisher
Elsevier B.V.
Type
Article
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Abstract
Alkaline phosphatase from rat osseous plate is allosterically modulated by ATP, calcium and magnesium at pH 7.5. At pH 9.4, the hydrolysis of ATP and PNPP follows Michaelis-Menten kinetics with K0.5 values of 154 muM and 42 muM, respectively. However, at pH 7.5 both substrates exhibit more complex saturation curves, while only ATP exhibited site-site interactions. Ca2+-ATP and Mg2+-ATP were effective substrates for the enzyme, while the specific activity of the enzyme for the hydrolysis of ATP at pH 7.5 was 800-900 U/mg and was independent of the ion species. ATP, but not PNPP, was hydrolyzed slowly in the absence of metal ions with a specific activity of 140 U/mg. These data demonstrate that in vitro and at pH 7.5 rat osseous plate alkaline phosphatase is an active calcium or magnesium-activated ATPase.
Description
Keywords
ALLOSTERIC MODULATION, Alkaline phosphatase, ATPase, ENZYME KINETICS
Language
English
Citation
Biochimica Et Biophysica Acta. Amsterdam: Elsevier B.V., v. 1202, n. 1, p. 22-28, 1993.
