Peroxyl-oxidized Erythrocyte Membrane Band 3 Protein with Anion Transport Capacity is Degraded by Membrane-bound Proteinase
Author:
Publisher
Informa UK Limited
Subject
General Medicine,Biochemistry
Link
http://www.tandfonline.com/doi/pdf/10.1080/10715760400000992
Reference17 articles.
1. Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3
2. Structure and function of the cytoplasmic domain of band 3: center of erythrocyte membrane—peripheral protein interactions
3. Mechanism of Free Radical-Induced Hemolysis of Human Erythrocytes: Hemolysis by Water-Soluble Radical Initiator
4. Presence of membrane-bound proteinases that preferentially degrade oxidatively damaged erythrocyte membrane proteins as secondary antioxidant defense
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1. Anion exchange through band 3 protein in canine leishmaniasis at different stages of disease;Pflügers Archiv - European Journal of Physiology;2017-04-05
2. SO4 = uptake and catalase role in preconditioning after H2O2-induced oxidative stress in human erythrocytes;Pflügers Archiv - European Journal of Physiology;2016-12-17
3. Grape Epicatechin Conjugates Prevent Erythrocyte Membrane Protein Oxidation;Journal of Agricultural and Food Chemistry;2012-04-13
4. Effect of pre-exposure of human erythrocytes to oxidants on the haemolytic activity of Sticholysin II. A comparison between peroxynitrite and hypochlorous acid;Free Radical Research;2010-11-30
5. Stycholysin II, a cytolysin from the sea anemone Stichodactyla helianthus promotes higher hemolysis in aged red blood cells;Toxicon;2008-06
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