Chapter 7 - Mass Transport Flashcards
(101 cards)
Haemoglobin structure
Haemoglobin is a water soluble globular protein with a quaternary structure
How many polypeptide chains does haemoglobin have?
Describe structure of haemoglobin
Four polypeptide chains- each bonded to a haem group which contains an iron ion (Fe2+)
What is haemoglobin bound to oxygen is called?
Oxyhaemoglobin
What is positive cooperativity?
When one oxygen moleucle binds, the quaternary structure changes to make it easier for other oxygen molecules to bind. Sme happens for disassociation too, for oxygen to unbind.
Slightly harder for 4th oxygen molecule to bind because harder to find a binding site
There are four polypeptide chains each binded to a haem group that contains one iron ion
How many oxygen molecules can one iron ion bind to?
Therefore how many oxygen molecules can a haemoglobin molecule carry?
Each polypeptide chain is bonded to a haem group that contains an ion of iron, which is able to bind to one oxygen molecule.
So one haemoglobin molecule can bind to 4 oxygen molecules
Oxygen molecules bind one at a time.
Describe what each structure of the haemoglobin is ?
Primary - sequence of amino acids in the four polypeptide chains
Secondary- each of the four chains is coiled into a helix
Tertiary- polypeptide chain is folded into a precise shape which helps with its function
Quaternary - All four polypeptide chains are linked- contains haem groups and iron ions.
What is the process in which hameglobin binds with oxygen called and where does it occur?
Loading/ Associating
Happens in lungs
What is the process in which haemoglobin releases/unbinds its oxygen and where does it occur?
Unloading/ Disossiating
Happens in tissues
How does positive cooperativity affect association and dissociation
Allows oxygen to rapidly associated and dissociate from haemoglobin
Why do different haemoglobins have different affinities to oxygen and how does this affect association?
Diff haemoglobin molecules have slightly diff amino acid sequences so different shapes- shape can cause the haemoglobin to have either a high or low affinity for oxygen
Haemoglobin with a high affinity for oxygen take up more oxygen easily but release it less easily
Those with low affinity for oxygen take up oxygen less easily but release it more easily
Partial pressure of oxygen-What is it?
Amount of oxygen that is present in a mixtyre of gases
measured by the pressure it contributes to the total pressure of the gas mixture
measure in kilopascals
Oxygen always moves from high to low partial pressure.
How does partial pressure affect oxygen association and dissociation?
When partial pressure is high, Leaving the lungs, oxygen diffuses downits pressure gradient and binds to haemoglobin in a process called oxygen association.
In respiring tissues, the partial pressure of oxygen islow. Oxygen diffuses down its pressure gradient and unbinds from haemoglobin in a process called oxygen dissociation when pp is low
The partial pressure of oxygen is lowest in the respiring tissues and highest in the lungs. Positive cooperativity is involved in increasing the rate of both binding and unbinding between oxygen and haemoglobin.
As the partial pressure of oxygen increases, the percentage saturation of haemoglobin with oxygen…
also increases
What is the percentage saturation of haemoglobin
The percentage saturation of haemoglobin with oxygen is a measure of how many iron ions in the haemoglobin molecules are bound to oxygen
What does oxygen dissociation curve show?
The relationship between the percentage saturation of haemoglobin and the partial pressure of oxygen
(Curve flashcard is on quizlet) - saturation on y should go from 0 to 100
partial pressure on x
Explain the shape of the oxygen dissociation curve
Explain why goes flat, steep then flat.
The increase in gradient is due to positive cooperativity. When an oxygen molecule binds to haemoglobin, it makes it easier for another oxygen molecule to bind. This causes the percentage saturation of haemoglobin with oxygen to increase rapidly.
Steep gradient is due to positive copperativity
At higher partial pressures, the curve flattens - plateaus at around 98% saturation- This is because as it reaches full saturation it is harder for oxygen to find an empty binding site
How does carbon dioxide affect the curve?
The lower the conc of carbon dioxide in the blood, the further left the curve is
The greater the conc of carbon dioxide, the more readily haemoglobin releases its oxygen, curve further to the right
At lower carbon dioxide concentrations, oxygen…?
Associates more readily
Dissociates less readily
Because it has a greater percentage saturation of haemoglobin
Vice versa for high conc of carbon dioxide
What is the Bohr Effect?
The curve shifiting left or right as a result of a change in conc of carbon dioxide
Carbon dioxide and pH
How does it affect acidity
At the gas exchange surfacel, C02 is constantly being removed
At a low conc of C02, the pH is slightly raised, less acidic
At a high conc of C02, the pH is lowered, more acidic
So curves to the right have higher acidity
How does the C02 increase acidity
Carbon dioxide reacts with water in our blood to form H+ ions, more H+ ions means more acidic
How does acidity affect the haemoglobin?
What happens to association/dissocitation when acidic and alkali?
Haemoglobin molecules are proteins, so changes in acidity can change the shape of the haemoglobin molecule - changes shgape of tertiary strcutre
When acidic, easier for oxygen to dissociate
When less acidic, easier for oxygen to associate
Why is the Bohr effect beneficial for exercise
Respiring muscle cells release carbon dioxide, which decreases the pH of the blood near the tissues. This causes haemoglobin to change shape, allowing oxygen to dissociate more readily. As a result, cells are provided with more oxygen for aerobic respiration.
Explain the advantage of the changes seen in the haemoglobin of people with anaemia- who have a lower conc of haemoglobin in the blood
At every measured partial pressure of oxygen, the percentage saturation of haemoglobin with oxygen is lower in people with anaemia. This corresponds to a shift in the oxyhaemoglobin dissociation curve to the right. It means that haemoglobin releases oxygen more readily in the tissues for respiration. This allows the body to meet its energy demands despite having less haemoglobin in the blood.
What does higher affinity mean?
Haemoglobin has a higher affinity for oxygen
Where does this happen and what ph?
Associates more readily and dissociates less readily
‘haemoglobin likes oxygen’
Happens in lungs bc there is a lower conc of c02-higher pH