3.4.1-Mass Transport Animals Flashcards
- Describe the structure of haemoglobin. Why do we say it has quaternary structure? (Q2 Jan 2011)
It is a protein made of 4 polypeptide chains (two alpha chains and two beta chains)
Each polypeptide chain has a heme group which is where the oxygen molecule binds.
(One haemoglobin molecules can hold up to 4 oxygen molecules)
It has a quaternary structure because it is made of more than 1 polypeptide chain
- Write an equation to show the reversible reaction between haemoglobin and oxygen
Haemoglobin + oxygen oxygaemoglobin
Hb + 4O2 Hb(O2)4
nnotate this graph stating where oxygen is loaded and unloaded and wh
- Annotate this graph stating where oxygen is loaded and unloaded and why (Q7 June 2010)
- Give the formula for calculating the percentage saturate of haemoglobin with oxygen
Percentage saturate of haemoglobin with oxygen = Oxygenated haemoglobin x 100
Maximum saturation
- How does the binding of the first oxygens to haemoglobin affect the affinity of haemoglobin? (Use the term tertiary structure in your answer)
- 1 Oxygen molecule binds to haemoglobin;
- This alters tertiary structure of Hb;
- Uncovers second binding site for haem group to bind to;
- This increases the affinity of Hb to Oxygen (so it’s easier for the 2nd and 3rd molecules of oxygen to bind)
- This is called cooperative binding
- Sketch a curve on the graph above to show what happens when carbon dioxide levels increase (sh
curve on the graph above to show what happens when carbon dioxide levels increase (shown in red)
Organisms which are adapted to permanently live at high altitude (BIOL2 Q2 Jan 2011)
Shift to the left
Allows oxygen to be LLLLOADED even at low partial pressures of oxygen
Humans who have gone to live at high altitude (and thus have a higher number of red blood cells than humans who live at sea level) (BIOL2 Q4 Jan 2010)
Shift to the right
Allows oxygen to be RRRRELEASED to respiring cells so that organisms can maintain a high metabolic rate
Large mammal with small SA:Vol ratio
BIOL2 June 2010 Q7
Shift to the left
These organisms lose very little heat due to their small SA:Vol ratio. Therefore they do not require a high rate of respiration and muscle contraction to keep them warm. So their rate of respiration is low
So curve shifted to the left to so haemoglobin hoLLLLLds onto the oxygen
Small mammal with large SA:Vol ratio
BIOL2 June 2010 Q7
Shift to the right
These organisms lose a lot of heat due to their large SA:Vol ratio. Therefore the high rate of respiration and muscle contraction generate heat to keep them warm. This requires a high rate of respiration
So curve shifted to the right means that oxygen is RRRRELEASED to respiring cells
Foetal haemoglobin
Shift to the left
The curve shifted to the left so foetal haemoglobin has a higher affinity for oxygen than adult haemoglobin
This means that at the same partial pressure of oxygen, the adult haemoglobin can unload oxygen and the foetal haemoglobin can LLLLLOAD oxygen
Myoglobin
Myoglobin
Shift to the left
Myoglobin is found in muscles The curve shifted to the left so myoglobin has a higher affinity for oxygen than normal haemoglobin
This means that at the same partial pressure of oxygen, the haemoglobin can unload oxygen and the myoglobin can LLLLOAD oxygen
This allows myoglobin to act as a ‘store’ of oxygen
Heart
Name of organ Name of blood vessel entering organ Name of blood vessel leaving organ
Heart From the lungs = pulmonary vein
From the body = vena cava To the lungs = pulmonary artery
To the body = aorta
Liver
From the heart = Hepatic artery
From the small intestine = hepatic portal vein Hepatic vein
Kidney
Renal artery Renal vein