M103 T2 L1 Flashcards
What is oxygen’s blood solubility like?
it’s poorly soluble
only a small amount is directly dissolved in the water of the plasma
Can pO2 be normal in a patient with hypoxia?
yes - bc there is no Hb to carry oxygen
What is the equation for respiration in muscle tissue?
C6H12O6 + 6O2 = 6CO2 + 6H2O + 36 ATP
What is the equation for anaerobic glycolysi?
C6H12O6 = 2 lactate + 2ATP
What percentage of the dry weight of an RBC is Hb?
95%
How many daltons is a haem group and a peptide in Hb?
small haem group - 616 Da
large globin peptide - 17,000 Da
What is the structure of haem like?
rigid, 2D and highly coloured porphyrin ring
How does co-operativity affect how affinity for additional uptake of o2 into Hb?
the allosteric effect means each subunit influences its 3 neighbours - it increases their affinity for O2 increases due to shape change
What types of Hb do adults have?
HbA - 99%
HbF - 1%
Which two factors affect Hb affinity for O2 and why?
increased blood CO2 and decreased blood pH
these are conditions in hard working muscles and allows Hb to lose affinity for O2 and offload it into the tissues
How does the carbolic anhydrase reaction affect blood pH?
it increases co2 blood levels
so there is a decreases in blood pH
What three modes are used to transport co2 in the blood?
10% dissolved
22% as carbamino
68% as HCO3-
What happens during chloride shift?
a co2 mlc (in deoxy muscle) enters Hb, and reacts to make an acid and carbonates which are removed from Hb in exchange for Cl-
What happens to chloride shift when the deoxygenated blood reaches the lungs?
it reverses - H+ reforms into co2 and carbonate, the latter re-enters the Hb mlc in exchange for the removal of Cl-
What is the normal pO2 of the lungs?
100 mmHg
What are the graph shapes of myoglobin and Hb?
Hb - sigmoidal
myoglobin - hyperbolic
An increase in which molecules causes a Hb dissociation curve to rightward - shift?
co2, pH and Cl-
2,3-DPG
How does 2,3-DPG cause rightward-shift?
it binds to Hb, lowering its affinity for O2
How does HbF react to 2,3-DPG compared to maternal Hb?
HbF has a lower affinity for 2,3-DPG compared to maternal Hb
HbF therefore has a higher affinity for o2 instead
Explain the graph shape of myoglobin
has very high affinity; small amounts of oxygen just immediately fill up the myoglobin until it’s nearly totally full. There’s very little change after a certain level
Since normal Hb has a lower o2 affinity than myoglobin and HbF, how is it still effective?
a normal Hb mlc will be less avid to the o2 - will give away some of the oxygen. If that o2 just sits there, the Hb will go into EQL with the o2 concentration
However, if the Hb releases the o2 and it is then hoovered up by the myoglobin or by maternal haemoglobin, the Hb tries to get into EQL.
there’s very little oxygen in the plasma nearby because every time the Hb releases an oxygen, that oxygen is hoovered up out of the plasma and onto another bound to another molecule, either to the higher affinity, foetal haemoglobin or myoglobin.
What are the conditions in active muscles (during exercise)?
O2 is low, CO2 is high
Blood is slightly acidic due to co2 and lactic acid
Temperature is higher
There is myoglobin (left-shifted saturation vs Hb)