ISSN:
1572-8773
Keywords:
alkaline phosphatase
;
manganese ions
;
osseous plate
;
Polidocanol
;
p-nitrophenylphosphate
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
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 μ m) were inhibitory. Manganese ions could play the role of zinc ions stimulating the enzyme synergistically in the presence of magnesium ions (K d = 7.2 μ m; 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 (K d = 2.2 μ m; 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00156163
Permalink
