Peroxidase Properties of Extracellular Superoxide Dismutase-Reference-Cited by-同舟云学术

Peroxidase Properties of Extracellular Superoxide Dismutase

Published:2002-09 Issue:9 Volume:22 Page:1402-1408
ISSN:1079-5642
Container-title:Arteriosclerosis, Thrombosis, and Vascular Biology
language:en
Short-container-title:ATVB

Author:

Hink H. Ulrich¹,Santanam Nalini¹,Dikalov Sergey¹,McCann Louise¹,Nguyen Andrew D.¹,Parthasarathy Sampath¹,Harrison David G.¹,Fukai Tohru¹

Affiliation:

1. From the Division of Cardiology, Department of Medicine (H.U.H., S.D., L.M., A.D.N., D.G.H., T.F.), and the Department of Gynecology and Obstetrics (N.S., S.P.), Emory University School of Medicine, and the Atlanta Veterans Administration Hospital (L.M., D.G.H., T.F.), Atlanta, Ga.

Publisher

Ovid Technologies (Wolters Kluwer Health)

Subject

Cardiology and Cardiovascular Medicine

Reference42 articles.

1. Interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide. Inactivation of the enzyme

2. A new look at a time-worn system: oxidation of CuZn-SOD by H2O2

3. Nitration of -tocopherol and oxidation of -tocopherol by copper-zinc superoxide dismutase/H2O2/NO2-: Role of nitrogen dioxide free radical

4. Bicarbonate Enhances the Hydroxylation, Nitration, and Peroxidation Reactions Catalyzed by Copper, Zinc Superoxide Dismutase

5. Bicarbonate Enhances the Peroxidase Activity of Cu,Zn-Superoxide Dismutase

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