Interaction of haptoglobin with hemoglobin octamers based on the mutation αAsn78Cys or βGly83Cys

Octameric hemoglobins have been developed by the introduction of surface cysteines in either the alpha or beta chain. Originally designed as a blood substitute, we report here the structure and ligand binding function; in addition the interaction with haptoglobin was studied. The recombinant Hbs (rH...

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Hlavní autoři: Brillet, Thomas, Marden, Michael C., Yeh, Joanne I., Shen, Tong-Jian, Ho, Nancy T., Kettering, Regina, Du, Shoucheng, Vasseur, Corinne, Domingues-Hamdi, Elisa, Ho, Chien, Baudin-Creuza, Véronique
Médium: Artigo
Jazyk:Inglês
Vydáno: 2012
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3706102/
https://ncbi.nlm.nih.gov/pubmed/23847747
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.4236/ajmb.2012.21001
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