3B Haemoglobin Flashcards
Where is haemoglobin found and what is its function?
It is found in red blood cells and its role is to carry oxygen around the body.
What animals have haemoglobin?
All vertebrates, and also earthworms, starfish, some insects and plants, and some bacteria.
Describe the structure of haemoglobin.
Haemoglobin is a large protein with a quaternary structure.
It is made up of four polypeptide chains.
Describe the properties of the polypeptide chains in haemoglobin.
Each chain has a haem group which contains an iron ion an gives haemoglobin its red colour.
How many molecules of oxygen can a single haemoglobin molecule carry?
Four.
What is haemoglobin called when it combines with oxygen?
Where does this occur and what is this process called?
In the lungs.
This is called association or loading.
Oxyhaemoglobin is formed.
What molecule is formed when oxygen leaves oxyhaemoglobin?
Where does this occur and what is this process called?
This occurs near body cells in respiring tissue.
The process is called dissociation or unloading.
The oxyhaemoglobin becomes haemoglobin again.
What is the equation for the processes of unloading and loading of oxygen on haemoglobin?
Hb + 4O2 HbO8
What is affinity for oxygen?
The tendency a molecule has to bind with oxygen.
Describe partial pressure of oxygen (pO2)
This is one of the conditions that affects haemoglobin’s affinity for oxygen.
It is a measure of oxygen concentration, ie. the concentration of dissolved oxygen in cells.
How does pO2 affect haemoglobin’s affinity for oxygen?
As pO2 increases, haemoglobin’s affinity for oxygen increases.
Describe the pO2 when haemoglobin is loading and unloading oxygen.
In the lungs there’s a high pO2 as oxygen enters through the alveoli. Oxygen loads onto haemoglobin to form oxyhaemoglobin.
When cells respire they use up oxygen, so in respiring tissue there’s a lower pO2. Red blood cells deliver oxyhaemoglobin to these tissues where it unloads its oxygen.
What does an oxygen dissociation curve show?
How saturated haemoglobin is with oxygen at any given partial pressure.
How does affinity for oxygen affect saturation of oxygen?
The higher the affinity for oxygen the more saturated the haemoglobin is with oxygen, and vice versa.
How does saturation of oxygen affect affinity of haemoglobin, and how does this change the shape of the dissociation curve?
When haemoglobin first combines with an oxygen molecule its shape changes making it easier for other molecules to join, too. But eventually the haemoglobin becomes so saturated that it gets harder for oxygen molecules to join. As a result the curve is steeper in the middle- S shaped.