Familial secondary erythrocytosis due to increased oxygen affinity is caused by destabilization of the T state of hemoglobin Brigham (α2β2Pro100Leu)

Protein Science

Volumn 21, Issue 10, 2012, Pages 1444-1455

  Mollan, Todd L ^a   Abraham, Bindu ^a   Strader, Michael Brad ^a   Jia, Yiping ^a   Lozier, Jay N ^b   Olson, John S ^c   Alayash, Abdu I ^a  

^a CENTER FOR BIOLOGICS EVALUATION AND RESEARCH   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

^c RICE UNIVERSITY   (United States)

Author keywords

Allostery; Hemoglobin; Kinetics; Ligand binding

Indexed keywords

HEMOGLOBIN; HEMOGLOBIN BRIGHAM; UNCLASSIFIED DRUG;

ADULT; ALKALINITY; AMINO ACID SUBSTITUTION; ARTICLE; BOHR EFFECT; CASE REPORT; ERYTHROCYTE; ERYTHROCYTOSIS; ESCHERICHIA COLI; FAMILIAL SECONDARY ERYTHROCYTOSIS; FEMALE; HEMOLYSATE; HUMAN; LIGAND BINDING; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MUTATION; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE;

ADULT; CHROMATOGRAPHY, REVERSE-PHASE; FEMALE; HEMOGLOBINS; HEMOGLOBINS, ABNORMAL; HUMANS; KINETICS; OXYGEN; POLYCYTHEMIA; RECOMBINANT PROTEINS;

ESCHERICHIA COLI;

EID: 84866599472     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2130     Document Type: Article

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