3.3.4 Mass Transport Flashcards
(128 cards)
What is the function of a red blood cell?
To transport oxygen around the body to respiring cells via the blood.
What is the protein found in red blood cells?
Haemoglobin
What is Haemoglobin?
A quaternary structure protein that is found in red blood cells. It is a group of chemically similar molecules that are found in many different organisms.
What is a quaternary protein?
Has more than one polypeptide (Haemoglobin has 4)
Describe the structure of Haemoglobin?
It is a quaternary protein with 4 polypeptide chains
It has 2 alpha polypeptide chains and 2 beta polypeptide chains
Each polypeptide is bound to one heme group
Heme groups have iron within them so is where oxygen binds to
This means Haemoglobin can bind to 4 oxygen molecules to form oxyhemoglobin
Why are Haemoglobin different in different organisms?
Because Haemoglobin is a group of proteins of different types, which differ slightly across different organisms (eg. Based on their environment).
What is affinity?
The ability of Haemoglobin to attract or bind to oxygen
Where in the body does Haemoglobin have a high affinity/low affinity or oxygen?
High affinity in the lungs- to load oxygen to transport it around the body
Low affinity at respiring cells- to unload oxygen needed for respiration
How does Haemoglobin change its affinity?
By altering its tertiary structure depending on its location in the body eg. Due to a change in pH
What is saturation?
When Haemoglobin is holding the maximum amount of oxygen it can bind to.
What is association/loading?
The binding of oxygen to Haemoglobin
Describe association of oxygen and Haemoglobin?
Each heme group picks up one oxygen molecule so Haemoglobin can carry 4 oxygen molecules at a time.
It occurs when oxygen concentration is high and carbon dioxide concentration is low, as this increases Haemoglobin’s affinity for oxygen.
This results in association to form oxygen and Haemoglobin.
What is dissociation/unloading?
The detaching or unbinding of oxygen from Haemoglobin
Describe dissociation of oxyhaemoglobin?
Occurs when oxygen concentration is low and carbon dioxide concentration is high
Haemoglobin has a low affinity for oxygen
Results in dissociation to form oxygen and Haemoglobin
What is partial pressure?
Refers to the measure of oxygen concentration (pressure exerted by oxygen molecules).
Where is partial pressure of oxygen high/low and how does this affect the saturation of Haemoglobin?
Partial pressure of oxygen is high in the lungs due to a high concentration of oxygen. This means haemoglobin is unsaturated.
Partial pressure of oxygen is low in respiring tissues due to a low concentration of oxygen. This means haemoglobin is unsaturated.
What units is partial pressure measured in?
KPa
Describe how DNA changes haemoglobins affinity for oxygen?
DNA base sequence determines amino acid sequence of the polypeptide in the primary structure.
This changes the secondary structure depending on amino acids present, and so whether a-helix or b-sheets form.
Tertiary structure changes based on R groups of the amino acids in the primary sequence, and therefore determines how the polypeptide folds.
This determines how it conjugates with other polypeptides in the quaternary structure.
The different shaped quaternary structure proteins form different types of haemoglobin that each have a different affinity for oxygen.
What does the oxyhaemoglobin dissociation curve show?
The relationship between partial pressure of oxygen and percentage saturation of haemoglobin.
Haemoglobin is unsaturated at low partial pressure of oxygen as oxygen is unloaded.
Respiring tissues have a low partial pressure of oxygen as oxygen is used up in respiration.
Haemoglobin is saturated at high partial pressure of oxygen as oxygen is loaded.
Lungs have a high partial pressure of oxygen as it is inhaled there.
The graph shows how a small change in partial pressure of oxygen results in a large change in saturation (it has a sigmoidal/s-shape)
Describe co-operative binding/positive co-operativity?
Oxygen molecules do not all bind at the same time.
When the first oxygen molecule binds, haemoglobin changes shape (undergoes conformational changes).
This makes it easier for subsequent oxygens to bind as it uncovers new binding sites for oxygen.
When the third oxygen molecule binds, haemoglobin changes shape again.
This makes it more difficult for the 4th oxygen to bind.
It is also more difficult due to a lower partial pressure of oxygen than at first.
What is the Bohr effect?
The effect of carbon dioxide concentration on the oxygen dissociation curve for adult human haemoglobin.
What is the effect of a high carbon dioxide concentration on the oxyhaemoglobin curve and affinity?
It causes it to shift to the right, and affinity of haemoglobin for oxygen to decrease.
With carbon dioxide, haemoglobin is less saturated at a given partial pressure of oxygen, which shows it has a lower affinity for oxygen as it unloads more readily.
Explain the Bohr effect?
When respiration rate increases, a higher concentration of carbon dioxide is produced.
When carbon dioxide dissolves in the water in blood, it forms carbonic acid.
This means blood becomes acidic (decrease in blood pH).
Carbonic acid dissociates to produce H+ ions which decreases the pH of the blood plasma.
This changes the bonds in the tertiary structure of haemoglobin, and therefore its affinity for oxygen.
It means it has a lower affinity for oxygen at respiring cells to provide oxygen (and even lower during exercise due to faster rate of respiration during exercise).
Application of the Bohr effect in the human body?
At respiring cells, there is a high concentration of carbon dioxide.
This means haemoglobin has a low affinity for oxygen.
Therefore it unloads oxygen readily for respiration.
This means the curve shifts right.
At the alveoli/lungs, there is a low concentration of carbon dioxide.
This means haemoglobin has a high affinity for oxygen.
Therefore it loads oxygen readily to be transported to respiring cells.
This means the curve shifts left.