Báo cáo khoa học: Dimer asymmetry and the catalytic cycle of alkaline phosphatase from Escherichia coli
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Although alkaline phosphatase (APase) fromEscherichiacolicrystallizes as a symmetric dimer, it displays deviationsfrom Michaelis–Menten kinetics, supported by a modeldescribing a dimeric enzyme with unequal subunits [Orha-novic´ S., Pavela-Vrancˇicˇ M. and Flogel-Mrsˇic´ M. (1994)Acta. Pharm.44, 87–95]. The possibility, that the observedasymmetry could be attributed to negative cooperativity inMg2+binding, has been examined. The influence of themetal ion content on the catalytic properties of APase fromE. colihas been examined by kinetic analyses. ...
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Báo cáo khoa học: Dimer asymmetry and the catalytic cycle of alkaline phosphatase from Escherichia coli
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Báo cáo khoa học: Dimer asymmetry and the catalytic cycle of alkaline phosphatase from Escherichia coli
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