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A0157

Sigma-Aldrich

Ascorbate Oxidase from Cucurbita sp.

lyophilized powder, 1,000-3,000 units/mg protein

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Synonym(s):
L-Ascorbate:oxygen oxidoreductase, Ascorbase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

biological source

plant (Cucurbita spp.)

Quality Level

form

lyophilized powder

specific activity

1,000-3,000 units/mg protein

storage temp.

2-8°C

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This Item
P4105F7296189724
form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized

specific activity

1,000-3,000 units/mg protein

specific activity

≥35 units/mg protein (biuret)

specific activity

≥0.45 units/mg protein

specific activity

≥1500 U/mg, ≥300 units/mg material

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

-

Quality Level

100

General description

Ascorbate oxidase is a homodimeric enzyme, which comprises 552 amino acid residues per subunit (zucchini). It corresponds to a molecular mass of 70kDa per subunit. This enzyme is mainly found in plants, fungi and eubacteria.

Application

Ascorbate Oxidase from Cucurbita sp. has been used:
  • as a supplement in the culture medium for differentiation into osteoblasts
  • to oxidize ascorbic acid producing monodehydroascorbate in monodehydroascorbate reductase assay
  • in determining ascorbate (AsA) and dehydroascorbate (DHA) concentrations

Ascorbate oxidase, from Cucurbita sp., may be used to study oxidative stress and heat stress response and tolerance. Ascorbate oxidase, from Sigma, has been used in ascorbic acid assays to study the heat stress response of Arabidopsis .

Biochem/physiol Actions

Ascorbate oxidase (AO) participates in cell growth by regulating reduction/oxidation (redox) of the apoplast. This enzyme can synthesize the oxidative molecule dehydroascorbate acid (DHA) in the apoplast. It is also involved in cell elongation and enlargement development.
Ascorbate oxidase converts ascorbic acid to dehydroascorbic acid. It is highly specific for L-ascorbic acid and a few analogs. Ascorbate oxidase exists as a dimer and has a molecular weight of approximately 140 kDa.

Unit Definition

One unit will oxidize 1.0 μmole of L-ascorbate to dehydroascorbate per min at pH 5.6 at 25 °C.

Physical form

Lyophilized powder containing buffers and sucrose as stabilizer.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Ethylene response factor 6 is a regulator of reactive oxygen species signaling in Arabidopsis
Sewelam N, et al.
PLoS ONE, 8(8), e70289-e70289 (2013)
Irina I Panchuk et al.
Plant physiology, 129(2), 838-853 (2002-06-18)
To find evidence for a connection between heat stress response, oxidative stress, and common stress tolerance, we studied the effects of elevated growth temperatures and heat stress on the activity and expression of ascorbate peroxidase (APX). We compared wild-type Arabidopsis
Ann Wambui Munyaka et al.
Journal of food science, 75(4), C336-C340 (2010-06-16)
The thermal stability of vitamin C (including l-ascorbic acid [l-AA] and dehydroascorbic acid [DHAA]) in crushed broccoli was evaluated in the temperature range of 30 to 90 degrees C whereas that of ascorbic acid oxidase (AAO) was evaluated in the
Sudhakar Srivastava et al.
Protoplasma, 248(4), 805-815 (2010-12-29)
Arsenic (As) is a potential hazard to plants' health, however the mechanisms of its toxicity are yet to be properly understood. To determine the impact of redox state and energetic in stress imposition, plants of Hydrilla verticillata (L.f.) Royle, which
A Messerschmidt et al.
Journal of molecular biology, 224(1), 179-205 (1992-03-05)
The crystal structure of the fully oxidized form of ascorbate oxidase (EC 1.10.3.3) from Zucchini has been refined at 1.90 A (1 A = 0.1 nm) resolution, using an energy-restrained least-squares refinement procedure. The refined model, which includes 8764 protein

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