Transport of respiratory gases Flashcards
How is O2 transported around the body?
- Through red blood cells that contain the oxygen-binding protein haemoglobin
Explain the structure and adaptations of haemoglobin.
- Composed of 4 polypeptide chains and 4 heme groups
- Quaternary structure
- Contains prosthetic group (iron) to hold the structure together
- It can carry 4 O2 molecules and 1 CO2
- O2 binds to the heme group
- Depending on the surrounding O2 concentration, it can pick up or drop off O2
Explain the affinity for oxygen.
- As O2 molecules bind to the haemoglobin, the more the shape of the haemoglobin is changed
- This makes the binding easier, more likely to gain O2 (high affinity)
- The haemoglobin will have a higher affinity for O2 in a O2-rich environment, promotes oxygen loading
- In a low O2 environment (body tissues) haemoglobin has a lower affinity for oxygen
Why does the affinity decrease when there are less O2 molecules binded to the haemoglobin?
- When the haemoglobin drops off the O2 at a cell, it no longer wants to bind to the O2, since it is now needed by the cell
- The more oxygen is present, the more it wants to bind (e.g. in the lungs)
- The haemoglobin must be full
What does an oxygen dissociation curve show?
- The relationship between oxygen levels (as partial pressure) and O2 % saturation of haemoglobin
- The O2 % saturation of haemoglobin says how many haemoglobins are full of O2
- The partial pressure: the more O2 the higher the pressure
- Look curve from right to left
- When the haemoglobin moves through the body, the concentration (partial pressure) decreases because the O2 is needed by the tissues
- The % saturation decreases too, most O2 used up
What is foetal haemoglobin and its trend in the curve?
- Inside a fetus
- O2 binds with a higher affinity (high O2 environment) because foetal haemoglobin will load O2 when adult haemoglobin is unloading it in the placenta
- At lower partial pressures, it loses O2 easier than adult haemoglobin
- Has more affinity for O2 than adult
- Rapid dissociation of O2, since its concentration decreases
- Curve is to the left of adult haemoglobin
What is adult haemoglobin and its trend in the curve?
- Rapid saturation (uptake) of oxygen in lungs
- Rapid dissociation of O2 as its concentration decreases
- Loses O2 easier, low affinity (low O2 environment)
What is Myoglobin and its trend in the curve?
- Positioned to the left of the foetal haemo.
- Higher affinity for O2 than adult haemo.
- Only releases O2 when O2 is at very low concentrations in tissues (found in muscles)
- Hangs onto O2 longer than normal
- Tertiary structure, 1 polypeptide (1 heme group)
What determines the difference in shape of the adult haemoglobin and myoglobin dissociation curve?
- The cooperative effect of four heme groups in haemoglobin
- Haemoglobin has 4 heme groups and myoglobin has 1
- The oxygenation of each haemoglobin chain causes structural changes that increase the afffinity to gain O2
- Myoglobin has a higher affinity to allow it to gain O2 at low partial pressure in the muscles and only release when necessary
How do you analyse the oxygen dissociation curve for haemoglobin and myoglobin?
- Myoglobin has a higher affinity for oxygen (more likely to take up O2) than adult haemoglobin. Myoglobin takes up O2 at lower levels (normal takes up at high O2 levels)
- It holds on to its supply until levels in the muscles are very low
- The delayed released helps slow the inset of anaerobic respiration and lactic acid formation during exercise
How is CO2 transported around the body?
- Its a waste product and diffuses out of the cell.
- Small amounts are dissolved in the plasma
- Some binds with haemoglobin in the erythrocyte (RBC) to form HbCO2
- 70% of CO2 is transformed in RBC into hydrogen carbonate ions
How is CO2 converted into carbonic acid?
- CO2 enters the RBC and reacts with water. This reaction is catalysed by carbonic anhydrase to form carbonic acid H2CO3-
- Carbonic acid dissociates into H+ ions and hydrogen carbonate ions (HCO3-) a.k.a bicarbonate ions
See reactions in boook
How do hydrogen carbonate ions affect the pH? What does the chloride shift do?
- The HCO3- decreases the pH (more acidic). This increases breathing rate to remove the CO2
- The H+ ions in the RBC (erythrocyte) make the environment more acidic, causes haemoglobin to release its O2
- The bicarbonate leaves the RBC to enter the plasma. To balance the electric charge, Cl- ions enter the RBC by diffusion (chloride shift)
- Plasma proteins maintain the pH range, they act as buffers
What is the optimal pH range?
- 7.35-7.45
What effect do plasma proteins have?
- They act as buffers to resist change to pH by removing excess H+ ions (H+ ions make it more acidic)
- Maintains the pH of the blood in a optimal range
- The amino acids have the amine group that may take the H+ ions while the carboxyl group may release H+ ions
What does the Bohr shift show?
- It explains the increased release of O2 by haemoglobin in respiring tissues
- CO2 lowers the pH of the blood, which causes haemoglobin to release O2
- Decrease in PH shifts the curve to the right
- Haemoglobin is encouraged to release its oxygen at the regions of greatest need
What are chemoreceptors and what can they trigger?
- Positioned in the aorta and detect decreased pH levels
- Sensitive to changes in blood pH and can trigger body responses in order to maintain a balance
- The rate of ventilation (breathing) can increase, it can lower the concentration of CO2 in the blood
- Kidneys can control the reabsorption of bicarbonate (HCO3-) ions from the blood, clear excess in the urine
What controls the rate of ventilation?
- Medulla oblongata (respiratory control centre) responds to stimuli from chemoreceptors
What happens during exercise that changes the breathing rate?
- Chemoreceptors send signals to the medulla when it has detected changes in CO2 levels (more CO2, lower pH)
- The medulla increases the signals to the intercostal muscles and diaphragm to increase frequency of contractions, increase breathing rate
- Decreases CO2 levels in the blood, restore pH
What is the total lung capacity, residual volume and the tidal volume?
- Total lung capacity: maximum amount of air in lungs (6dm3)
- Residual volume: amount of air that remains in the lungs
- Tidal volume: amount of air breathed in and out in normal breathing (0.5dm3)
How does high altitude effect gas exchange?
- At high altitude, the amount of O2 does not change, but the partial pressure is lower
- This means the O2 molecules are more spread out and diffusion in the alveoli is less efficient
- More difficult for haemoglobin to take up and transport O2
What are short term adaptations for high altitudes?
- Ventilation rate increases, heart rate increases
- Symptoms such as fatigue, headaches and rapid pulse
- Blood vessels dilate
- Mountain sickness
What are long term adaptations (acclimatisation) for high altitudes?
- More RBC and haemoglobin, to maximize O2 uptake and leads to higher affinity
- More blood vessels, better O2 supply
- Muscles will produce more myoglobin, more storage
- Greater lung surface area and larger chest sizes
What are benefits of high altitude training?
- Increased stamina
- Increased sprint speed
- Increased RBC (erythrocytes)
- More haemoglobin
- More mitochondria in muscles
- More gaseous exchange