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Purification and molecular properties of ascorbate peroxidase from bovine eye.

Abstract：

:Ascorbate peroxidase (APX) is a hydrogen peroxide-scavenging peroxidase which uses ascorbate (AsA) as the specific electron donor. APX has not been isolated in mammals. Ocular tissue contains AsA at high concentrations, and we detected APX activity in bovine retinal pigment epithelium (RPE) and choroid. We purified APX from bovine RPE and choroid by four chromatographic steps. The purified APX was a monomeric hemoprotein with a molecular mass of 43 kDa. The amino acid sequence of the amino-terminal region of the purified APX showed a high degree of homology to that of plants. The primary product of the APX reaction was identified as the monodehydroascorbate radical. The APX showed high specificity for AsA as an electron donor. This is the first isolation and characterization of APX from mammals, and its role in the protection against active species of oxygen in ocular tissue is discussed.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Wada N,Kinoshita S,Matsuo M,Amako K,Miyake C,Asada K

doi

10.1006/bbrc.1997.7946

subject

Has Abstract

pub_date

1998-01-14 00:00:00

pages

256-61

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(97)97946-8

journal_volume

242

pub_type

杂志文章

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