dc.contributorUniversidade de São Paulo (USP)
dc.contributorUniversidade Estadual Paulista (UNESP)
dc.date.accessioned2022-04-28T19:53:48Z
dc.date.accessioned2022-12-20T01:43:08Z
dc.date.available2022-04-28T19:53:48Z
dc.date.available2022-12-20T01:43:08Z
dc.date.created2022-04-28T19:53:48Z
dc.date.issued1990-01-01
dc.identifierInternational Journal of Biochemistry, v. 22, n. 7, p. 747-751, 1990.
dc.identifier0020-711X
dc.identifierhttp://hdl.handle.net/11449/223914
dc.identifier10.1016/0020-711X(90)90010-Z
dc.identifier2-s2.0-0025036202
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/5404043
dc.description.abstract1. 1. The inhibition of matrix-induced alkaline phosphatase by zinc ions is due to the displacement of magnesium ions from its binding site. 2. 2. Binding of magnesium ions to alkaline phosphatase induces conformational changes which activate the enzyme. 3. 3. Binding of zinc ions to alkaline phosphatase induces conformational changes which impair the catalytic action of the enzyme. 4. 4. The inhibition of the enzyme by zinc ions is affected by membrane environment and magnesium ions. © 1990.
dc.languageeng
dc.relationInternational Journal of Biochemistry
dc.sourceScopus
dc.titleEffect of membrane moiety and magnesium ions on the inhibition of matrix-induced alkaline phosphatase by zinc ions
dc.typeArtículos de revistas


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