Pregled bibliografske jedinice broj: 982107
Evidence for asymmetry of alkaline phosphatase from E.coli
Evidence for asymmetry of alkaline phosphatase from E.coli // Acta pharmaceutica, 44 (1994), 1; 87-95 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 982107 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Evidence for asymmetry of alkaline phosphatase from E.coli
Autori
Stjepan Orhanović ; Maja Pavela-Vrančić ; Mirna Flogel-Mršić
Izvornik
Acta pharmaceutica (1330-0075) 44
(1994), 1;
87-95
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
alkaline phosphatase ; asymmetry ; curve fitting
Sažetak
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.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
POVEZANOST RADA
Ustanove:
Farmaceutsko-biokemijski fakultet, Zagreb,
Prirodoslovno-matematički fakultet, Split
Citiraj ovu publikaciju:
Časopis indeksira:
- Scopus