The mechanism of formation, structure and physiological relevance of covalent hemoglobin attachment to the erythrocyte membrane

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• 作者：Elizabeth M. Welbourn^a ; ^{ewelbo@essex.ac.uk} ; Michael T. Wilson^a ; Ashril Yusof^b ; Metodi V. Metodiev^a ; Chris E. Cooper^a ; ^{ccooper@essex.ac.uk}
• 关键词：AE1 ; Anion Exchanger 1 (band 3 protein) ; BSA ; (bovine serum albumin) ; CO ; carbon monoxide ; Co-IP ; co-immunoprecipitation ; DTT ; dithiothreitol ; Hb ; hemoglobin ; KCN ; potassium cyanide ; NEM ; N-ethyl maleimide ; PBS ; phosphate buffered saline pH 7.4 ; Prx2 ; peroxiredoxin-2 ; SOSG ; singlet oxygen sensor green
• 刊名：Free Radical Biology and Medicine
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：103
• 期：Complete
• 页码：95-106
• 全文大小：1303 K
• 卷排序：103

文摘

Hemoglobin binding to membranes initiated by mild oxidative stress. More binding of hemoglobin to membranes at higher oxidation state (Fe III to Fe V). Bound hemoglobin is redox active and retains ability to bind ligands. Bound complex contains spectrin, ankyrin and band 4.2. Bound complex is formed in vivo following extreme endurance exercise.