Abstract
Polidocanol-solubilized osseous plate alkaline phosphatase was modulated by cobalt ions in a similar way as by magnesium ions. For concentrations up to 1 μM, the Chelex-treated enzyme was stimulated by cobalt ions, showing K d = 6.0 μM, V = 977.5 U/mg, and site-site interactions ( n = 2.5). Cobalt-enzyme was highly unstable at 37°C, following a biphasic inactivation process with inactivation constants of about 0.0625 and 0.0015 min−1. Cobalt ions stimulated the enzyme synergistically in the presence of magnesium ions ( K d = 5.0 μM; V = 883.0 U/mg) or in the presence of zinc ions ( K d =75.0 μM; V= 1102 U/mg). A steady-state kinetic model for the modulation of enzyme activity by cobalt ions is proposed.
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