Literature DB >> 6477937

Characterization of alkaline phosphatase inactivation by ascorbic acid.

G A Miggiano, A Mordente, G E Martorana, E Meucci, A Castelli.   

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.

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Year:  1984        PMID： 6477937     DOI： 10.1016/0167-4838(84)90190-0

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  4 in total

1.  The relationship between the optical properties and the kinetic behaviour of ascorbate-inhibited alkaline phosphatase.

Authors:  G E Martorana; E Meucci; A Ursitti; G A Miggiano; A Mordente; A Castelli
Journal:  Biochem J       Date:  1986-12-15       Impact factor: 3.857

2.  Purification and characterization of a specific nucleoside diphosphatase from soybean root nodules.

Authors:  H D Doremus; D G Blevins
Journal:  Plant Physiol       Date:  1988-05       Impact factor: 8.340

3.  Characterization of nucleoside triphosphatase activity in isolated pea nuclei and its photoreversible regulation by light.

Authors:  Y R Chen; S J Roux
Journal:  Plant Physiol       Date:  1986       Impact factor: 8.340

4.  Effect of Humid Air Exposed to IR Radiation on Enzyme Activity.

Authors:  Olga I Yablonskaya; Vladimir L Voeikov; Kirill N Novikov; Ekaterina V Buravleva; Valeriy A Menshov; Aleksei V Trofimov
Journal:  Int J Mol Sci       Date:  2022-01-06       Impact factor: 5.923
  4 in total

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