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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
Properties
GENERAL: hemoglobin-variant
RELATED: hemoglobin S/beta thalassemia +
hemoglobin S/beta thalassemia 0
sickle cell trait
sickle cell disease
sickle cell
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