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KMID : 0380219940270040342
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Journal of Biochemistry and Molecular Biology
1994 Volume.27 No. 4 p.342 ~ p.345
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Kinetic Properties of Rat Intestinal Phytase/Alkaline Phosphatase
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Abstract
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Abstract:
@EN The regulatory properties of phytase/alkaline phosphatase purified from rat intestine were investigated. Alkaline phosphatase activity was significantly inhibited by phenylalanine, while phytase activity was not affected. Both activities were
similarly inhibited by inorganic phosphate, a product of the enzyme reactions, although the modes of inhibition were different. The inhibition of phytase activity was noncompetitive, while the inhibition of alkaline phosphatase activity was
competitive.
Vanadate, a nonspecific inhibitor of phosphatases, strongly inhibited alaline phosphatase activity but the inhibition of phytase activity was moderate. Phytate, the substrate for phytase, inhibited alkaline phosphatase activity biphasically. At
lower
concentrations inhibition was mild and competitive, but it became strong at higher concentrations. In addition, the heat stabilities of the two activities were also different with incubation at 50℃ for 20 min, 90% of the initial alkaline
phosphatase
activity was lost while loss of phytase activity was negligible. These results suggest that the active sites for the two activities are not identical.
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