Understanding the molecular basis of the high oxygen affinity variant human hemoglobin Coimbra

Human hemoglobin (Hb) Coimbra (βAsp99Glu) is one of the seven βAsp99 Hb variants described to date. All βAsp99 substitutions result in increased affinity for O2 and decreased heme-heme cooperativity and their carriers are clinically characterized by erythrocytocis, caused by tissue hypoxia. Since βA...

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Detalles Bibliográficos
Autores principales: Jorge, S.E., Bringas, M., Petruk, A.A., Arrar, M., Marti, M.A., Skaf, M.S., Costa, F.F., Capece, L., Sonati, M.F., Estrin, D.
Formato: JOUR
Materias:
Allostery
Hb Coimbra
Hemoglobin variant
Oxygen affinity
Polycythemia
hemoglobin coimbra
hemoglobin hotel dieu
hemoglobin kempsey
hemoglobin radcliffe
hemoglobin variant
hemoglobin yakima
hemoglobin ypsilanti
oxygen
phytic acid
unclassified drug
2,3 diphosphoglyceric acid
heme
hemoglobin Coimbra
allosterism
Article
blood viscosity
computer simulation
conformational transition
controlled study
dissociation rate constant
erythrocytosis
hemolysate
human
hypoxemia
molecular dynamics
molecular probe
oximetry
oxygen affinity
priority journal
protein function
protein modification
chemistry
genetics
in vitro study
kinetics
metabolism
molecular model
protein domain
protein quaternary structure
2,3-Diphosphoglycerate
Allosteric Regulation
Heme
Hemoglobins, Abnormal
Humans
In Vitro Techniques
Kinetics
Models, Molecular
Molecular Dynamics Simulation
Oxygen
Phytic Acid
Protein Interaction Domains and Motifs
Protein Structure, Quaternary
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00039861_v637_n_p73_Jorge
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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