Peroxide-Induced Oxidative Modification of Hemoglobin.,Doklady Biochemistry and Biophysics

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Peroxide-Induced Oxidative Modification of Hemoglobin.
Doklady Biochemistry and Biophysics ( IF 0.8 ) Pub Date : 2019-07-31 , DOI: 10.1134/s1607672919030116
A D Vasilyeva ₁ , L V Yurina ₁ , A E Bugrova ₁ , M I Indeykina _{1,

2} , D Y Azarova _{1,

3} , A V Bychkova ₁ , K I Akzhigitova _{1,

4} , A S Kononikhin _{1,

2,

5} , E N Nikolaev _{1,

5,

6} , M A Rosenfeld ₁

Affiliation

Abstract

The oxidative modification of human hemoglobin (Hb) treated with hydrogen peroxide was investigated. Using the mass spectrometry method, the oxidized amino acid residues of the hemoglobin molecule were detected: αTrp14, αTyr24, αArg31, αMet32, αTyr42, αHis45, αHis72, αMet76, αPro77, αLys90, αCys104, αTyr140, βHis2, βTrp15, βTrp37, βMet55, βCys93, βCys112, βTyr130, βLys144, and βHis146. The antioxidant potential of the Hb molecule in the intracellular space and in the blood plasma is discussed.

中文翻译：

过氧化物诱导的血红蛋白的氧化修饰。

摘要

研究了过氧化氢对人血红蛋白（Hb）的氧化修饰。使用质谱法检测血红蛋白分子的氧化氨基酸残基：αTrp14，αTyr24，αArg31，αMet32，αTyr42，αHis45，αHis72，αMet76，αPro77，αLys90，αCys104，αTyr140，βHis2，βTrp15，βTet15，βTet15 βCys93，βCys112，βTyr130，βLys144和βHis146。讨论了Hb分子在细胞内空间和血浆中的抗氧化潜力。

更新日期：2019-07-31

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