Haemoglobin Flashcards
(28 cards)
Why can’t oxygen be carried in the blood as it is
Solubility of oxygen in aqueous solutions is low
More efficient to have the oxygen-carrying molecule haemoglobin
How many molecules of haemoglobin does an erythrocyte carry
300 million
Haemoglobin
A quaternary protein Composed of four subunits Each containing a haem group (Fe2+) Has an affinity for oxygen Carries oxygen in the blood
Affinity
Chemical attraction
What is formed when oxygen and haemoglobin combine
Oxyhaemoglobin
Percentage saturation of haemoglobin
Oxygenated haemoglobin/Maximum saturation x 100
Partial pressure of oxygen
The amount of oxygen in a mixture of gas or solution
pO2/kPa
Lower pO2
Less haemoglobin saturated with oxygen
Where is the low partial pressure of oxygen
Tissues/respiring cells
Around 5kPa at rest
Where is the high partial pressure of oxygen
In lungs
Around 16kPa
In capillaries around 13.16kPa
Loading/association
When oxygen is taken up by haemoglobin
Unloading/dissociation
When oxygen is released/given up by haemoglobin
When is oxygen unloaded
In low oxygen concentrations
Low pO2/kPa
So it can be used by respiring cells/tissues
When does Hb have a higher affinity for oxygen
At high partial pressures of oxygen
Explain the cooperative nature of oxygen loading
The first oxygen molecule binding to Hb alters its three D tertiary structure
Exposing the 2nd and 3rd binding sites
So it is easier for the 2nd and 3rd oxygen molecules to bind and load
Oxygen dissociation curve name of shape
Sigmoid
Hb maximum saturation
98%
When red blood cells pass through the pulmonary capillaries
Explain the importance of the pO2 in tissues
Low due to aerobic respiration
Hb has a lower affinity for O2 at lower pO2 so oxyhaemoglobin starts to break down and oxygen is unloaded
How does the oxygen dissociation curve provide evidence for the cooperative nature of oxygen loading
At low pO2 there is little increase in saturation as oxygen increases
Then a rapid increase as it gets easier for 2nd and 3rd oxygen molecules to bind
Explain the effect of increased respiration on oxygen dissociation
Tissue cells respire anaerobically
Reducing the dissolved oxygen in the surrounding tissue fluid
Reducing partial pressure to a level lower than normal
Oxygenated blood with fully saturated haemoglobin unloads oxygen more readily
Due to Hb now having a lower affinity to oxygen because of low kPa
More oxygen unloaded at respiring cells for respiration to provide ATP for muscle contraction
What is the effect of carbon dioxide in the blood
Dissolves in the blood
Making it more acidic and lowering pH
Since Hb is a protein the change in pH slightly alters its tertiary structure
So it has a lower affinity to O2 at high levels of pCO2
Explain the Bohr shift
Higher than normal pCO2 causes oxygen dissociation curve to shift to the right
CO2 makes blood more acidic so changes the shape of the protein Hb
Reducing its affinity to oxygen
And decreasing the saturation for the same pO2
Since the pO2 will be high at respiring cells, more oxygen will be unloaded
To be used for aerobic respiration to produce ATP
To meet the demands of oxygen of the organisms cells
Explain the relationship between surface area to volume ratio of mammals and the effect of this on the oxygen dissociation curve of their Hb
Smaller mammals have a greater surface area to volume ratio
So more more heat lost per unit mass
Smaller mammals have a greater rate of respiration/metabolism
Oxygen is required for this aerobic respiration
So Hb unloads oxygen more readily at the tissues because has a lower affinity for oxygen
Shifts to right
What does a steep oxygen dissociation curve mean
Oxygen unloaded more readily in small decreases of oxygen