| Literature DB >> 7865996 |
F A Leone1, P Ciancaglini, J M Pizauro, A A Rezende.
Abstract
Polidocanol-solubilized osseous plate alkaline phosphatase was modulated by manganese ions in a similar way as by zinc ions. For concentrations up to 1.0 nM, the enzyme was stimulated by manganese ions, showing site-site interactions (n = 2.2). However, larger concentrations (> 0.1 microns) were inhibitory. Manganese ions could play the role of zinc ions stimulating the enzyme synergistically in the presence of magnesium ions (Kd = 7.2 microns; V = 1005.5 U mg-1). Manganese ions could also play the role of magnesium ions, stimulating the enzyme synergistically in the presence of zinc ions (Kd = 2.2 microns; V = 1036.7 U mg-1). However, manganese ions could not substitute for zinc and magnesium at the same time since ion assymetry is necessary for full activity of the enzyme. A steady-state kinetic model for the modulation of enzyme activity by manganese ions is proposed.Entities:
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Year: 1995 PMID： 7865996 DOI： 10.1007/bf00156163
Source DB: PubMed Journal: Biometals ISSN： 0966-0844 Impact factor: 2.949