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Updated: Jun 19, 2026

A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells

A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells

Published on: April 11, 2014

ON THE INACTIVATION OF ASCORBIC ACID OXIDASE.

W H Powers¹, C R Dawson

¹Department of Chemistry, Columbia University, New York.

The Journal of General Physiology

|October 30, 2009

Summary

This summary is machine-generated.

Ascorbic acid oxidase rapidly inactivates during ascorbic acid oxidation. Protective agents like catalase and peroxidase prevent this reaction inactivation, suggesting a role for reactive oxygen species.

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Published on: March 18, 2012

Area of Science:

Biochemistry
Enzymology

Background:

Ascorbic acid oxidase is crucial for ascorbic acid oxidation.
Enzyme inactivation during reaction can limit experimental outcomes.

Purpose of the Study:

Investigate the causes of ascorbic acid oxidase inactivation during ascorbic acid oxidation.
Identify protective agents and mechanisms against this inactivation.

Main Methods:

Enzymatic oxidation of ascorbic acid using purified ascorbic acid oxidase.
Measurement of oxygen uptake to quantify enzyme inactivation.
Addition of various substances (proteins, metal complexes) to assess protective effects.

Main Results:

Ascorbic acid oxidase undergoes rapid inactivation during ascorbic acid oxidation.
Environmental factors contribute minorly, while an inherent system factor, possibly reactive oxygen, is the major cause.
Native catalase, peroxidase, methemoglobin, and hemin significantly protect the oxidase.
Protective agents do not interfere with oxygen uptake or hydrogen peroxide removal.

Conclusions:

Ascorbic acid oxidase inactivation is primarily an intrinsic property of the reaction system.
Reactive oxygen species are implicated in the inactivation process.
Specific iron-porphyrin compounds offer protection, highlighting potential mechanisms for enzyme stabilization.