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Evidence for asymmetry of alkaline phosphatase from E.coli (CROSBI ID 259955)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Stjepan Orhanović ; Maja Pavela-Vrančić ; Mirna Flogel-Mršić Evidence for asymmetry of alkaline phosphatase from E.coli // Acta pharmaceutica, 44 (1994), 1; 87-95

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

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Podaci o izdanju

44 (1)

1994.

87-95

objavljeno

1330-0075

1846-9558

Povezanost rada

Kemija

Indeksiranost