Chapter 7 Flashcards
What is the primary structure of haemoglobin?
The sequence of amino acids in the four polypeptide chains.
What is the secondary structure of haemoglobin?
How each polypetide chain is coiled into a helix
What is the tertiary structure of haemoglobin?
Is each polypeptide chain is coiled into a precise shape
What is the quarternary structure of haemoglobin?
How all four polypeptide chains are linked together to form a spherical molecule. Each polypeptide is assoicated with a haem group, which contains a ferrous (Fe 2+ ion). Each ferrous ion can combine with one O2 molecule.
What is the process of loading oxygen?
Where haemoglobin binds/associates with O2 in the lungs.
What is the process of unloading oxygen?
Where haemoglobin releases/dissociates with it’s O2 in the tissues.
What is an affinity for oxygen?
High affinity more readily binds with O2 but releases it less easily.
Low affinity less easily binds with O2 but releases it more readily.
How is haemoglobin efficient at transporting oxygen?
- Must readily associate with O2 at the surface where gas exchange takes place.
- Must readily dissociate from O2 at those tissues requiring.
How does haemoglobin change shape to be efficient at transporting O2?
It shape changes in the presence of CO2 to bind more loosely and so releases O2.
What is an oxygen dissociation curve?
The graph of the relationship between between the saturation of haemoglobin with O2 and oxygens partial pressure
Why does little O2 bind to haemoglobin when O2 concentrations are low, how does this refelct on graph?
The shape of the haemoglobin molecule makes it difficult for the first O2 molecule to bind to one of the sites on it’s four polypetide chains as they are so closely united. This initailly creates a shallow curve
What happens when the first O2 molecule binds to haemoglobin?
The binding of the initial O2 molecule changes the quarternary structure of the haemoglobin molecule. This change makes it easier for the other sub units to bind to O2.
What is meant by the term positve co-operativity?
Binding of the second O2 molecule requires a smaller partial pressure than the first
What happens to haemoglobin after the third O2 molecule binds?
In theory it is easier fr haemoglobin to bind to the fourth O2 molecule, however with the majority of binding sites occupied it is less likely that an O2 molecule will bind to the empty one
How is the oxygen dissociation curve related to oxygen affinity?
The further left the curve is the greater the affinity of haemoglobin for O2.
The further right of the curve the lower the affinity of haemoglobin for O2.
What is the Bohr effect?
The greater the concentration of CO2, the more readily O2 is unloaded by haemoglobin
Why is the concentration of CO2 low at the gas exchange surface?
CO2 diffuses across the lungs and is excreted from the organism. Haemoglobins affinity for O2 is increased, and coupled with the high concentration of O2 in the lungs means O2 is readily loaded by haemoglobin. This reduces CO2 concentration
Why is the concentration of CO2 high in rapidly respiring tissues?
The affinity of haemoglobin for O2 is reduced, which couled with the low O2 concentrations means that O2 is readily unloaded from haemoglobin into the muscle cells. Increasing CO2 concentration.
Outline the process by which there is always enough O2 for respiring tissues?
- The higher the rate of respiration the more CO2 is produced.
- The more CO2 produced, the lower (more acidic) the PH.
- The lower PH leads to a greater change in the shape of haemoglobin, lowering it’s affinity for O2..
- The more readily O2 is unloaded, the more O2 is available for respiration.
Why do large organisms require a transport sysytem?
They have a low surface area to volume ratio and are very active
Name seven features of a transport system?
- A medium to tranport substances.
- A form of mass transport where the transport medium is moved in large distances
- A closed system of tubular vessels to contain the transport medium and form a branching network
- A mechanism for moving the transport medium within the vessels.
- A mechanism to maintain the mass flow movement in one direction
- A means of controlling the flow of transport to suit the dynamic needs of the organism
- A mechanism to support the mass flow, e.g. intercostal muscles