Sickle cell hemoglobin fiber structure altered by alpha-chain mutation.

Hybrid hemoglobin molecules prepared with beta chains from hemoglobin S (beta 6 Glu leads to Val) and alpha chains from hemoglobin Sealy (alpha 47 Asp leads to His) form fibers with a novel structure. In contrast to the typical fibers of hemoglobin S with an average diameter of 22 nm and a solid cro...

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Veröffentlicht in:	Proc Natl Acad Sci U S A
Hauptverfasser:	Crepeau, R H, Edelstein, S J, Szalay, M, Benesch, R E, Benesch, R, Kwong, S, Edalji, R
Format:	Artigo
Sprache:	Inglês
Veröffentlicht:	National Academy of Sciences 1981
Schlagworte:	Research Article
Online-Zugang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC319139/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6940165/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.78.3.1406
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