Lec 10 Erythrocyte Biochem Flashcards
Erythropoiesis steps
What are the subunits on hemoglobin?
2 alpha globin chains
2 beta globin chains
how many heme per subunit?
What form of iron in heme?
Function and characteristic of heme?
1
Ferrous Fe2+
Carries O2 and is hydrophobic
Types of heme?
Embryonic
fetal
adult
Embryonic heme
Gower and portland up to 8 weeks (embryo)
Fetal hemoglobin heme type and presence
HbF (alpha gamma)
At 10 weeks alpha and gamma rise gamma fall near birth
Adult heme and presence
HbA aplpha and beta
beta rises around birth alpha already present
Hb A2 rarer
sickle cell anemia heme and research
Hbs
research ongoing to induce expression of HbF
(hydroxyurea)
What binds to heme?
F8 histidine
(proximal histidine)
What stabalizes bond between heme and O2
Distal histamine (E7)
Conformational change
Myoglobin oxygen dissociation curve?
hyperbolic more to the left
Hemoglobin oxygen dissociation curve shape?
sigmoidal (due to interactions between subunits)
Cooperativity in hemoglobin
Oxygen dissociation curve (release of O2)
Bohr Effect
pH of active tissues lower
binding affinity decreases with pH
histidine is bound with H+
conformation chang of Hb favors O2 release
2,3 bisphosphoglycerate
reduces 02 affinity so Hb gives up O2 to tissues
signal Hb to let go of O2
the curve and exercise
has pO2 drop from 40 to 20 torr which is steepest part of curve so very effective in providing oxygen to tissues
The curve and HbF and HbA
Fetus needs Hb that has higher affinity for O2 than mothers (left shift)
HbF does not bind well to 2,3 BPG (cause for affinity diff)
Iron cycle basic process