L1 Flashcards
Oxygen is poorly soluble in plasma. How much more O2 can haemoglobin carry than is directly dissolved in plasma?
70x more
How many ATP is formed via anaerobic respiration in rbcs?
2 ATP
What percentage of a rbc is Hb?
95% dry weight
Each haemoglobin and myoglobin subunit has 1 haem group. Describe the structure of a haem group. (4)
porphyrin ring
2D
coloured (because of e- sharing and is NOT due to Fe2+)
bound to ferrous ion (Fe2+)
How many O2 molecules per haem?
1
Describe adult/maternal Hb (HbA)
2 alpha subunits
2 beta subunits
Describe foetal haemoglobin’s structure and properties (HbF)
2 alpha subunits
2 gamma subunits
binds O2 more strongly than adult haemoglobin
Why does an increase in blood CO2 level decrease the affinity of Hb for O2?
more CO2 = less O2 in cells -> less muscle contractions -> Hb encouraged to release O2 for muscle contraction
Why does a decrease in blood pH decrease the affinity of Hb for O2?
more acidic environment -> damaging to cells -> Hb encouraged to release O2 to raise blood pH to normal level
Give the equation for the formation of carbonic acid
H2O + CO2 –> H2CO3
What % of CO2 is:
dissolved?
transported as carbamino?
transported as HCO3-?
10%
22%
68%
Explain how CO2 can be transported in the blood as HCO3-
CO2 enters and combines with H2O to form H2CO3
this is broken down to H+ and HCO3-
HCO3- then exchanged for Cl- via the band 3 protein (chloride-bicarbonate exchanger)
Explain the chloride shift
(Chlorine hates gas)
(at the lungs) O2 enters rbc -> Cl- leaves and enters surrounding blood
(at the muscles) CO2 enters surrounding blood -> Cl- enters rbc
For O2 binding, describe the myoglobin curve and the haemoglobin curve
myo: hyperbolic/exponential
haemo: sigmoidal
Describe the effect of 2,3-diphosphopglycerate in HbA vs HbF
binds to Hb and lowers its for O2 for HbA but not HbF