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Kinetic Studies of Alkaline Phosphatase Extracted from Rabbit (Lepus townsendii) Liver

Author(s): V.O. Njoku | P.C. Chikezie | M.A. Kaoje | C.C. Monago | A.A. Uwakwe

Journal: Asian Journal of Biochemistry
ISSN 1815-9923

Volume: 6;
Issue: 1;
Start page: 65;
Date: 2011;
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Keywords: michealis-menten constant | Alkaline phosphatase | Lepus townsendii | 4-nitrophenylphosphate (4-NPP) | Arrhenius relationship

Lepus townsendii liver. Incubation of ALP extract with 4-nitrophenylphosphate (4-NPP) in glycine-NaOH buffer mixture at 37C for 30 min formed the basis for determination of enzyme activity. Spectrophotometric method was used to assay for the enzyme activity for 30 min and the kinetic constants-maximum enzyme velocity (Vmax) and Michealis-Menten constant (Km) were evaluated. The Km and Vmax values were 0.5x10-3 M and 20x10-6 M min-1, respectively. Inhibition studies showed that ALP activity was competitively inhibited by 0.67 mM sodium hydrogen orthophosphate (NaH2PO4) and the inhibition constant (Ki) was 0.9x10-3 M. The optimum pH value for ALP activity was about 9.2 and optimum temperature registered 45C. ALP activity exhibited linear Arrhenius relationship at temperature greater than 44.95C with corresponding catalytic energy of activation (Ea) = 15.23 KJ mole-1. The present study gave insights into characteristic catalytic properties of ALP extracted from L. townsendii liver.]]>
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