mass transport in humans Flashcards
(52 cards)
What are haemoglobins?
A group of chemically similar molecules found in many different organisms
Haemoglobins are essential for oxygen transport in various life forms.
What type of protein is haemoglobin?
A protein with a quaternary structure
This means it is composed of more than one polypeptide chain.
What is the primary role of haemoglobin?
Transport of oxygen in red blood cells
Haemoglobin carries oxygen from the lungs to body tissues.
What is the oxyhaemoglobin dissociation curve?
A graph that shows the loading, transport, and unloading of oxygen by haemoglobin
It illustrates how haemoglobin’s affinity for oxygen changes with different conditions.
What does cooperative binding mean in relation to haemoglobin?
The change in shape of haemoglobin upon binding the first oxygen makes it easier for additional oxygens to bind
This phenomenon enhances oxygen loading efficiency.
What is the Bohr effect?
The effect of carbon dioxide concentration on the dissociation of oxyhaemoglobin
Increased carbon dioxide lowers pH, promoting oxygen release from haemoglobin.
How do different animals adapt their haemoglobin?
By possessing different types of haemoglobin with varying oxygen transport properties
Adaptations help animals survive in their specific environments.
What is the composition of human haemoglobin?
Made up of four polypeptide chains, each containing a haem group with an iron ion
The iron ion is crucial for oxygen binding, giving haemoglobin its red color.
What occurs in the lungs regarding haemoglobin and oxygen?
Oxygen joins to haemoglobin to form oxyhaemoglobin in a reversible reaction
This process is essential for effective oxygen transport to tissues.
Define the terms ‘loading’ and ‘unloading’ in the context of haemoglobin.
‘Loading’ refers to the binding of oxygen to haemoglobin; ‘unloading’ refers to the release of oxygen from oxyhaemoglobin
These processes are critical for oxygen delivery to cells.
What does ‘affinity for oxygen’ mean?
The tendency of a molecule to bind with oxygen
Haemoglobin’s affinity varies with conditions such as oxygen concentration.
What is the relationship between partial pressure of oxygen (pO2) and haemoglobin’s affinity for oxygen?
As pO2 increases, haemoglobin’s affinity for oxygen also increases
This allows for efficient oxygen loading in the lungs.
What happens to oxygen during cellular respiration?
Cells deliver oxyhaemoglobin to tissues, where oxygen is unloaded
This process is vital for cellular metabolism.
Fill in the blank: Haemoglobin can carry _______ oxygen molecules.
four
Each haemoglobin molecule has the capacity to bind four molecules of oxygen.
True or False: Haemoglobin is found only in vertebrates.
False
Haemoglobin is also found in earthworms, some insects, plants, and bacteria.
What is the primary function of haemoglobin?
Transport oxygen around the body
Haemoglobin is a protein found in red blood cells that binds to oxygen for transport.
What happens to haemoglobin in the lungs?
Haemoglobin loads oxygen due to high oxygen concentration and high affinity
The high partial pressure of oxygen (pO₂) in the lungs allows haemoglobin to bind effectively with oxygen.
What occurs in respiring tissues regarding haemoglobin?
Haemoglobin unloads oxygen due to low oxygen concentration and low affinity
In tissues where oxygen is consumed, the partial pressure of oxygen is lower, leading to oxygen release.
What does the oxygen dissociation curve represent?
It shows how saturated the haemoglobin is with oxygen at any given partial pressure
The curve illustrates the relationship between pO₂ and the percentage saturation of haemoglobin.
What is the shape of the oxygen dissociation curve?
S-shaped
This shape indicates varying affinity of haemoglobin for oxygen based on saturation levels.
At what pO₂ level does haemoglobin have a high affinity for oxygen?
Where pO₂ is high, such as in the lungs
This results in high saturation of haemoglobin with oxygen.
At what pO₂ level does haemoglobin have a low affinity for oxygen?
Where pO₂ is low, such as in respiring tissues
This results in low saturation of haemoglobin with oxygen.
What is the significance of 100% saturation of haemoglobin?
Every haemoglobin molecule is carrying the maximum of 4 molecules of oxygen
This indicates optimal oxygen transport capacity.
What effect does saturation of haemoglobin have on its affinity for oxygen?
As haemoglobin becomes more saturated, it becomes harder for additional oxygen molecules to join
This results in the characteristic S-shape of the dissociation curve.