Alkaline phosphatase inactivation by mixed function oxidation systems

Alvaro Mordente; Giacinto A.D. Miggiano; Giuseppe E. Martorana; Elisabetta Meucci Calabrese; Stefano Angelo Santini; Adriano Castelli

doi:10.1016/0003-9861(87)90334-1

Alkaline phosphatase inactivation by mixed function oxidation systems

Alvaro Mordente, Giacinto A.D. Miggiano, Giuseppe E. Martorana, Elisabetta Meucci Calabrese, Stefano Angelo Santini, Adriano Castelli

Risultato della ricerca: Contributo in rivista › Articolo in rivista

32 Citazioni (Scopus)

Abstract

Alkaline phosphatase is inactivated by mixed function oxidation systems. OH. radicals, generated via an ascorbate-modified Haber-Weiss cycle or a Fenton-type reaction, seem to be responsible for the protein oxidative damage. Experiments with hydroxyl radical scavengers, enzyme substrates, products, and metal cofactors suggest that a "site-specific" radical attack takes place at or near the active center. Vitamin E fails to protect alkaline phosphatase; uric acid, instead, is particularly effective in shielding the protein against covalent modifications.

Lingua originale	English
pagine (da-a)	176-185
Numero di pagine	10
Rivista	Archives of Biochemistry and Biophysics
Volume	258
DOI	https://doi.org/10.1016/0003-9861(87)90334-1
Stato di pubblicazione	Pubblicato - 1987

Keywords

Alkaline Phosphatase
Antioxidants
Ascorbic Acid
Catalase
Cations, Divalent
Copper
Ferric Compounds
Ferrous Compounds
Free Radicals
Glutathione
Hydrogen Peroxide
Hydroxides
Hydroxyl Radical
Kinetics
Mercaptoethanol
Metals
Mixed Function Oxygenases
Oxidation-Reduction
Peroxidase
Superoxide Dismutase
Thiourea
Uric Acid
Vitamin E
Xanthine Oxidase

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10.1016/0003-9861(87)90334-1

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abstract = "Alkaline phosphatase is inactivated by mixed function oxidation systems. OH. radicals, generated via an ascorbate-modified Haber-Weiss cycle or a Fenton-type reaction, seem to be responsible for the protein oxidative damage. Experiments with hydroxyl radical scavengers, enzyme substrates, products, and metal cofactors suggest that a {"}site-specific{"} radical attack takes place at or near the active center. Vitamin E fails to protect alkaline phosphatase; uric acid, instead, is particularly effective in shielding the protein against covalent modifications.",

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doi = "10.1016/0003-9861(87)90334-1",

language = "English",

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T1 - Alkaline phosphatase inactivation by mixed function oxidation systems

AU - Mordente, Alvaro

AU - Miggiano, Giacinto A.D.

AU - Martorana, Giuseppe E.

AU - Meucci Calabrese, Elisabetta

AU - Santini, Stefano Angelo

AU - Castelli, Adriano

PY - 1987

Y1 - 1987

N2 - Alkaline phosphatase is inactivated by mixed function oxidation systems. OH. radicals, generated via an ascorbate-modified Haber-Weiss cycle or a Fenton-type reaction, seem to be responsible for the protein oxidative damage. Experiments with hydroxyl radical scavengers, enzyme substrates, products, and metal cofactors suggest that a "site-specific" radical attack takes place at or near the active center. Vitamin E fails to protect alkaline phosphatase; uric acid, instead, is particularly effective in shielding the protein against covalent modifications.

AB - Alkaline phosphatase is inactivated by mixed function oxidation systems. OH. radicals, generated via an ascorbate-modified Haber-Weiss cycle or a Fenton-type reaction, seem to be responsible for the protein oxidative damage. Experiments with hydroxyl radical scavengers, enzyme substrates, products, and metal cofactors suggest that a "site-specific" radical attack takes place at or near the active center. Vitamin E fails to protect alkaline phosphatase; uric acid, instead, is particularly effective in shielding the protein against covalent modifications.

KW - Alkaline Phosphatase

KW - Antioxidants

KW - Ascorbic Acid

KW - Catalase

KW - Cations, Divalent

KW - Copper

KW - Ferric Compounds

KW - Ferrous Compounds

KW - Free Radicals

KW - Glutathione

KW - Hydrogen Peroxide

KW - Hydroxides

KW - Hydroxyl Radical

KW - Kinetics

KW - Mercaptoethanol

KW - Metals

KW - Mixed Function Oxygenases

KW - Oxidation-Reduction

KW - Peroxidase

KW - Superoxide Dismutase

KW - Thiourea

KW - Uric Acid

KW - Vitamin E

KW - Xanthine Oxidase

KW - Alkaline Phosphatase

KW - Antioxidants

KW - Ascorbic Acid

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KW - Cations, Divalent

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KW - Oxidation-Reduction

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KW - Superoxide Dismutase

KW - Thiourea

KW - Uric Acid

KW - Vitamin E

KW - Xanthine Oxidase

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JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

ER -

Alkaline phosphatase inactivation by mixed function oxidation systems

Abstract

Keywords

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