Evidence for asymmetry of alkaline phosphatase from E.coli (CROSBI ID 259955)
Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija
Podaci o odgovornosti
Stjepan Orhanović ; Maja Pavela-Vrančić ; Mirna Flogel-Mršić
engleski
Evidence for asymmetry of alkaline phosphatase from E.coli
The steady-state kinetics of alkaline phosphatase from E. coli performed with pNPP as a substrate have been investigated. The enzyme shows deviation from Michaelis-Menten kinetics giving concave down Hanes plots. In the presence of a competitive substrate analogue, this effect become more pronounced. In an attempt to interpret the experimental data, non-linear regression fitting was applied to equations describing models, based on either negative cooperative interactions between subunits or independent nonequivalent active sites. The results obtained with pNPP as a substrate could not clearly differentiate between an allosteric and asymmetric model. however increased deviations observed in the presence of a substrate analogue could only be substantiated by a model assuming inherently nonequivalent subunits.
alkaline phosphatase ; asymmetry ; curve fitting
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano