Characterization of alkaline phosphatase inactivation by ascorbic acid

Ga Miggiano; Alvaro Mordente; Ge Martorana; Elisabetta Meucci Calabrese; A. Castelli

doi:10.1016/0167-4838(84)90190-0

Characterization of alkaline phosphatase inactivation by ascorbic acid

Ga Miggiano, Alvaro Mordente, Ge Martorana, Elisabetta Meucci Calabrese, A. Castelli^*

^*Autore corrispondente per questo lavoro

Facoltà di Medicina e Chirurgia "A.Gemelli"

Risultato della ricerca: Contributo in rivista › Articolo › peer review

7 Citazioni (Scopus)

Abstract

Ascorbic acid, isoascorbic acid and dehydroascorbic acid inhibit bovine kidney alkaline phosphatase activity. Ascorbic acid free radicals seem not to be involved. Dialysis does not make the inactivation reversible. A competitive mechanism can be inferred from experiments with phosphate and substrates, which block the activity decay. The influence of temperature, pH, other inhibitors and tertiary structure modifications on the inactivation process is also investigated.

Lingua originale	Inglese
pagine (da-a)	343-346
Numero di pagine	4
Rivista	BIOCHIMICA ET BIOPHYSICA ACTA
Volume	789
Numero di pubblicazione	3
DOI	https://doi.org/10.1016/0167-4838(84)90190-0
Stato di pubblicazione	Pubblicato - 1984

All Science Journal Classification (ASJC) codes

Biofisica
Biologia Strutturale
Biochimica
Biologia Molecolare

Keywords

Alkaline Phosphatase
Animals
Ascorbic Acid
Binding
Cattle
Competitive
Dehydroascorbic Acid
Hydrogen-Ion Concentration
Kidney
Structure-Activity Relationship
Temperature

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10.1016/0167-4838(84)90190-0

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abstract = "Ascorbic acid, isoascorbic acid and dehydroascorbic acid inhibit bovine kidney alkaline phosphatase activity. Ascorbic acid free radicals seem not to be involved. Dialysis does not make the inactivation reversible. A competitive mechanism can be inferred from experiments with phosphate and substrates, which block the activity decay. The influence of temperature, pH, other inhibitors and tertiary structure modifications on the inactivation process is also investigated.",

keywords = "Alkaline Phosphatase, Animals, Ascorbic Acid, Binding, Cattle, Competitive, Dehydroascorbic Acid, Hydrogen-Ion Concentration, Kidney, Structure-Activity Relationship, Temperature, Alkaline Phosphatase, Animals, Ascorbic Acid, Binding, Cattle, Competitive, Dehydroascorbic Acid, Hydrogen-Ion Concentration, Kidney, Structure-Activity Relationship, Temperature",

author = "Ga Miggiano and Alvaro Mordente and Ge Martorana and \{Meucci Calabrese\}, Elisabetta and A. Castelli",

year = "1984",

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TY - JOUR

T1 - Characterization of alkaline phosphatase inactivation by ascorbic acid

AU - Miggiano, Ga

AU - Mordente, Alvaro

AU - Martorana, Ge

AU - Meucci Calabrese, Elisabetta

AU - Castelli, A.

PY - 1984

Y1 - 1984

N2 - Ascorbic acid, isoascorbic acid and dehydroascorbic acid inhibit bovine kidney alkaline phosphatase activity. Ascorbic acid free radicals seem not to be involved. Dialysis does not make the inactivation reversible. A competitive mechanism can be inferred from experiments with phosphate and substrates, which block the activity decay. The influence of temperature, pH, other inhibitors and tertiary structure modifications on the inactivation process is also investigated.

AB - Ascorbic acid, isoascorbic acid and dehydroascorbic acid inhibit bovine kidney alkaline phosphatase activity. Ascorbic acid free radicals seem not to be involved. Dialysis does not make the inactivation reversible. A competitive mechanism can be inferred from experiments with phosphate and substrates, which block the activity decay. The influence of temperature, pH, other inhibitors and tertiary structure modifications on the inactivation process is also investigated.

KW - Alkaline Phosphatase

KW - Animals

KW - Ascorbic Acid

KW - Binding

KW - Cattle

KW - Competitive

KW - Dehydroascorbic Acid

KW - Hydrogen-Ion Concentration

KW - Kidney

KW - Structure-Activity Relationship

KW - Temperature

KW - Alkaline Phosphatase

KW - Animals

KW - Ascorbic Acid

KW - Binding

KW - Cattle

KW - Competitive

KW - Dehydroascorbic Acid

KW - Hydrogen-Ion Concentration

KW - Kidney

KW - Structure-Activity Relationship

KW - Temperature

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U2 - 10.1016/0167-4838(84)90190-0

DO - 10.1016/0167-4838(84)90190-0

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JF - BIOCHIMICA ET BIOPHYSICA ACTA

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ER -

Characterization of alkaline phosphatase inactivation by ascorbic acid

Abstract

All Science Journal Classification (ASJC) codes

Keywords

Accesso al documento

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