Ciancaglini, P.Pizauro, J. M.Leone, F. A.2014-05-202014-05-201995-11-15Journal of Inorganic Biochemistry. New York: Elsevier B.V. Publ Co Inc., v. 60, n. 3, p. 155-162, 1995.0162-0134http://hdl.handle.net/11449/31490Polidocanol-solubilized osseous plate alkaline phosphatase was modulated by cobalt ions in a similar way as by magnesium ions. For concentrations up to 1 mu M, the Chelex-treated enzyme was stimulated by cobalt ions, showing K-d = 6.0 mu M, V = 977.5 U/mg, and site-site interactions (n = 2.5). Cobalt-enzyme was highly unstable at 37 degrees 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 mu M; V = 883.0 U/mg) or in the presence of zinc ions (K-d = 75.0 mu M; V = 1102 U/mg). A steady-state kinetic model for the modulation of enzyme activity by cobalt ions is proposed.155-162engArtigo10.1016/0162-0134(95)00009-DWOS:A1995TE18000001Acesso restrito