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hemoglobin H
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
General
hemoglobin
Properties
COMPARTMENT: cytoplasm
CELL: erythrocyte
SUBUNITS: hemoglobin beta chain (4)
MOTIF: binding site
SITE: 2-2
FOR-BINDING-OF: 2,3-bisphosphoglycerate; via amino nitrogen
binding site
SITE: 3-3
FOR-BINDING-OF: 2,3-bisphosphoglycerate
lysine residue {60}
Iron [Fe]-binding site
SITE: 64-64
binding site
SITE: 83-83
FOR-BINDING-OF: 2,3-bisphosphoglycerate
MOTIF: lysine residue {83}
Iron [Fe]-binding site
SITE: 93-93
lysine residue {96}
leucine residue {142}
binding site
SITE: 144-144
FOR-BINDING-OF: 2,3-bisphosphoglycerate
lysine residue {145}
References
- Clinical Diagnosis & Management by Laboratory Methods,
J.B. Henry (ed), W.B. Saunders Co., Philadelphia,
PA. 1991, pg 650
- Medical Knowledge Self Assessment Program (MKSAP) 11, American
College of Physicians, Philadelphia 1998
Components
hemoglobin alpha chain (alpha globin, HBA1, HBA2)
hemoglobin beta chain (beta globin, HBB)
hemoglobin delta chain (delta-globin, HBD)
hemoglobin gamma chain