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hemoglobin S
Globin mutations may affect hemoglobin stability or oxygen affinity. Increased oxygen affinity:
1) low venous blood P50*
2) erythrocytosis Decreased oxygen affinity:
1) high venous blood P50*
2) diminished erythropoietin levels
3) physiological anemia
* pO2 at 50% hemoglobin saturation with oxygen
Laboratory: (diagnosis)
- hemoglobin electrophoresis
Related
hemoglobin S/beta thalassemia +
hemoglobin S/beta thalassemia 0
sickle cell
sickle cell (hemoglobin SS) disease
sickle cell trait; hemoglobin S trait
General
hemoglobin
Properties
COMPARTMENT: cytoplasm
CELL: erythrocyte
SUBUNITS: hemoglobin alpha chain (2)
MOTIF: lysine residue {12}
lysine residue {57}
Iron [Fe]-binding site
SITE: 59-59
lysine residue {61}
Iron [Fe]-binding site
SITE: 88-88
lysine residue {91}
lysine residue {100}
hemoglobin beta chain (2)
MOTIF: point mutation
SITE: RESIDUE-6
MUTATION-FROM-AMINO-ACID: glutamate residue
MUTATION-TO-AMINO-ACID: valine residue
heme-binding site
COFACTOR-BOUND: heme{FE+2}
FOR-BINDING-OF: O2
References
Clinical Diagnosis & Management by Laboratory Methods,
J.B. Henry (ed), W.B. Saunders Co., Philadelphia,
PA. 1991, pg 650
Components
hemoglobin alpha chain (alpha globin, HBA1, HBA2)
hemoglobin beta chain (beta globin, HBB)
hemoglobin delta chain (delta-globin, HBD)
hemoglobin gamma chain