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Mixed function oxidation and enzymes: kinetic and structural properties of an oxidatively modified alkaline phosphatase.

Abstract：

:No major structural alteration of alkaline phosphatase can be observed in the early stages of enzyme oxidative inactivation by the ascorbate model system. Fluorescence changes of protein-bound 8-anilino-1-naphthalenesulfonic acid suggest, however, that localized modifications take place. Oxidized alkaline phosphatase displays less catalytic efficiency (decrease of Vmax), while retaining the other kinetic properties, including the same affinity for substrates and inhibitors and the same activation energy of the native enzyme. Typical features of the modified protein are a decreased thermal stability and a biphasic heat inactivation profile, which make the oxidized form quite similar to aged enzymes. The lower response to Mg2+ activation indicates that the magnesium binding sites of alkaline phosphatase are probably the targets of the ascorbate system oxidative modifications.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Mordente A,Martorana GE,Miggiano GA,Meucci E,Santini SA,Castelli A

doi

10.1016/0003-9861(88)90315-3

subject

Has Abstract

pub_date

1988-08-01 00:00:00

pages

502-9

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(88)90315-3

journal_volume

264

pub_type

杂志文章

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