hemoglobin
Jump to navigation
Jump to search
Function
- oxygen transport protein of erythrocytes
- hemoglobin can bind up to 4 O2 molecules
- oxygen-binding capacity of 1.34 mL of O2 per gram of hemoglobin; this increases the total blood oxygen capacity ~ 70 fold compared to dissolved oxygen in blood
- carries 10% of CO2 in blood bound to globin chain
- carries nitric oxide (NO) bound to globin thiol
Structure
- tetramer, generally heterotetramer of
- 2 hemoglobin alpha chains
- 2 hemoglobin beta chains
- hemoglobin Barts in an exception
- each chain is associated with 1 heme moeity
Compartment
Expression
- expressed in erythrocytes & erythroid precursors
- hemoglobin is also found in
- CNS
- dopaminergic neurons in the substantia nigra
- astrocytes in the cerebral cortex & hippocampus
- mature oligodendrocytes
- outside CNS
- macrophages
- alveolar cells
- mesangial cells in the kidney
- CNS
Pathology
- see hemoglobinopathy
Laboratory
- hemoglobin in specimen
- hemoglobin in reticulocytes
- hemoglobin in body fluid
- hemoglobin electrophoresis
More general terms
More specific terms
- carboxyhemoglobin
- deoxyhemoglobin
- glycated hemoglobin
- hemoglobin A
- hemoglobin A2
- hemoglobin F
- hemoglobin Gower-1
- hemoglobin Gower-2
- hemoglobin Portland
- hemoglobin-variant
- methemoglobin (MetHb, Hi)
- oxyhemoglobin
- sulfhemoglobin
- unstable hemoglobin
Additional terms
- heme
- heme catabolism
- heme synthesis
- hemoglobin (Hgb) in blood
- hemoglobin electrophoresis
- hemoglobinopathy
- mean corpuscular hemoglobin concentration (MCHC)
References
- ↑ Alperts et al Molecular Biology of the Cell, Garland Publishing, New York, NY 1989 pg 289-291
- ↑ Wikipedia: Hemoglobin http://en.wikipedia.org/wiki/Hemoglobin