Kinetic Studies of Alkaline Phosphatase from the Liver of Agama agama Lizard
M.K. Abubakar, R.S.U. Wasagu and M.I. Umar.
Abstract
Kinetic studies were carried out on alkaline phosphatase (ALP) extracted from the liver of Agama agama lizard. Incubation of ALP extract with para nitrophenyl phosphate formed the basis for the determination of enzyme activity. Spectrophotometric method was used to assay the enzyme, and the kinetic constants: Maximum velocity (Vmax) and Michaelis Menten constant (Km) were calculated. The Km and Vmax values were 2.5mM and 1.538 X 10-3 µmol/min respectively. Inhibition studies show that the enzyme activity was competitively inhibited by 0.67mM sodium hydrogen orthophosphate (NaH2PO4) with inhibition constant (Ki) of 2.27mM. The optimum pH of the enzyme was 9.9 and the optimum temperature was 35OC. The enzyme exhibited linear Arrhenius relationship with corresponding catalytic energy of activation (Ea) of 1.44KJmol-1. This study gives an insight of the catalytic properties of ALP extracted from the liver of Agama agama lizard.
Key words: Alkaline phosphatase, Agama agama, para nitrophenyl phosphate (p - NPP), Arrhenius relationship, Michaelis Menten constant.
The articles in Bibliomed are open access articles licensed under Creative Commons Attribution 4.0 International License (CC BY), which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
We use cookies and other tracking technologies to work properly, to analyze our website traffic, and to understand where our visitors are coming from. More InfoGot It!
