3.4 Mass transport in animals Flashcards
(75 cards)
Describe the structure of haemoglobin
- Water soluble globular protein
- Consists of 4 polypeptide chains: 2 alpha chains and 2 beta chains
- Has 4 haem groups (prosthetic groups) containing iron (II) ions
- Oxygen molecules bind to the iron ions, forming oxyhaemoglobin
What is it called when haemoglobin gains oxygen and where does this happen
- Loading/ association
- Happens in the lungs
What is it called when haemoglobin loses oxygen and where does this happen
- Unloading/ dissociation
- Occurs in respiring tissues
What is affinity (in terms of oxygen and haemoglobin)
How likely haemoglobin is to bind to oxygen.
What affects the likelihood of oxygen binding to haemoglobin
- The partial pressure of oxygen which is a measure of oxygen concentration.
- The greater the partial pressure of oxygen, the more likely oxygen is to bind to haemoglobin.
What is partial pressure (of gases)
The pressure of a particular gas in a mixture, compared to the total pressure of all gases in the mixture.
Describe the oxygen dissociation curve
- x axis is partial pressure of oxygen
- y axis is saturation of haemoglobin with oxygen
- At lower partial pressures, haemoglobin has a low affinity for oxygen and vice versa
- The graph is an S shape as the relationship is not linear
Why is the shape of the oxygen dissociation curve not linear
- The first O2 does not bind easily with Hb (due to closely united polypeptide chains) so little O2 binds to Hb => gradient of curve is shallow.
- Binding of the first O2 changes the tertiary and quaternary structure, so easier for the 2nd and 3rd O2 to bind (positive cooperativity) => small increase in pO2 causes a big change in O2 saturation, shown by steep gradient
- After 3rd O2 binded, majority of binding sites/ haem groups are occupied, so O2 less likely to bind => less steep gradient
What are 2 factors that affect haemoglobin’s affinity for oxygen
- Partial pressure of oxygen
- Saturation of haemoglobin with oxygen
Why are there many different oxygen dissociation curves (2 reasons)
- The shape of haemoglobin can change under different conditions
- Different species have different haemoglobins with different affinities for oxygen
What does it mean if the oxygen dissociation curve is to the left of a human’s (and vice versa for the right)
The further left the curve is, the greater the affinity of haemoglobin for oxygen (O2 loads readily, unloads less readily) as the saturation of haemoglobin with oxygen is higher at lower partial pressures of oxygen.
What do more active organisms (like fish and birds) oxygen dissociation curves look like compared to human’s
- Their dissociation curves are shifted to the right
- This causes O2 to be able to dissociate from haemoglobin more readily
- This is needed as active organisms require a large amount of oxygen for respiration as activities like flying and swimming require a lot of energy
What do foetal dissociation curves look like compared to human’s
- Dissociation curve shifted to the left as lower partial pressure of oxygen in the womb
- Foetal Hb has a higher affinity for oxygen, causing association of O2 to occur more readily
Describe the relationship between oxygen dissociation curves and surface area to volume ratio (size of organism)
- Smaller organisms (larger surface area to volume ratio) have dissociation curves to the right of bigger organisms
- Larger Sa:V increases rate of heat loss to the environment, so need oxygen to be dissociated at a faster rate in order to increase the rate of respiration which is an exothermic reaction, so increases rate of heat production.
How does carbon dioxide affect the affinity of haemoglobin for oxygen and why (Bohr affect)
- When CO2 dissolves in water, it forms a carboxylic acid which affects the pH => more acidic in blood
- The change in pH causes haemoglobin to change shape which lowers the affinity
- This causes oxygen to dissociate more readily (in high concentrations of CO2)
When is the concentration of CO2 low and why is this useful
- Low near the lungs
- Causes Hb to have a high affinity for O2, so O2 associates more readily => blood becomes oxygenated
When is the concentration of CO2 high and why is this useful
- High near respiring tissues
- Causes Hb to have a low affinity for O2, so O2 dissociates more readily => oxygen released into cells for respiration
Describe the structure of myoglobin
Similar structure to haemoglobin, but only one haem group
Where is myoglobin found
In muscle cells
What is the use of myoglobin
- Acts as an oxygen reserve
- Has a very high affinity for oxygen, even at low partial pressures
- Oxygen will only dissociate from oxymyoglobin when partial pressures are very low (e.g. during intense muscular activity)
What are 4 common features of a circulatory system
- Suitable medium
- Means of moving the medium
- Mechanism to control the flow around the body
- Close system of vessels
What is the name of the circulatory system in mammals
Closed double circulatory system. It is ‘closed’ as it is confined to vessels and it is ‘double circulatory’ as blood passes through the heart twice for each complete circuit of the body.
Why do mammalian circulatory systems need to be double circulatory
- Mammals have a high metabolism
- Pressure of blood is reduced as it travels through the lungs (for more efficient gas exchange) so pressure needs to be increases to transport blood to the body quickly => pumps through the heart again to increase pressure.
What are the 2 groups of heart chambers called
Atrium and ventricles