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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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Bibliografske podrobnosti
Main Authors: 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
Format: Artigo
Jezik:Inglês
Izdano: 2012
Teme:
Online dostop: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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