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Substitutions in the β subunits of sickle-cell hemoglobin improve oxidative stability and increase the delay time of sickle-cell fiber formation

After reacting with hydrogen peroxide (H(2)O(2)), sickle-cell hemoglobin (HbS, βE6V) remains longer in a highly oxidizing ferryl form (HbFe(4+)=O) and induces irreversible oxidation of “hot-spot” amino acids, including βCys-93. To control the damaging ferryl heme, here we constructed three HbS varia...

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Detalles Bibliográficos
Autores principales:	Meng, Fantao, Kassa, Tigist, Strader, Michael Brad, Soman, Jayashree, Olson, John S., Alayash, Abdu I.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	American Society for Biochemistry and Molecular Biology 2019
Materias:	Bioenergetics
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6422104/ https://www.ncbi.nlm.nih.gov/pubmed/30630954 http://dx.doi.org/10.1074/jbc.RA118.006452

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