Mass transport (7) Flashcards
What is the structure of haemoglobin?
- globular
- water soluble
- 4 polypeptide chains each carrying a haem group (quaternary structure)
What is the role of haemoglobin?
O2 molecules bind to haem groups and are carried around body to where they are needed in respiring tissues
Where is haemoglobin found?
in red blood cells
What do oxyhaemoglobin dissociation curves show?
saturation percentage of haemoglobin with O2
plotted against partial pressure of O2 (kPa)
curve to left shows haemoglobin has high affinity for O2
What are 3 reasons for the mammalian circulatory system?
1) suitable medium for transport as it is water-based to allow substances to dissolve
2) means of maintaining pressure throughout body
3) means of controlling flow so it remains unidirectional such as valves
What is translocation?
where organic materials are transported around the plant
Why does O2 bind to haemoglobin in the lungs?
1) partial pressure of O2 is high
2) low concentration of CO2 in lungs so affinity is high
3) positive cooperativity
What is positive cooperativity?
after 1st O2 binds, binding of subsequent molecules is easier, but slightly harder for the 4th as there is low chance of finding a binding site
What are 3 factors affecting O2 and haemoglobin binding?
1) partial pressure/concentration of O2
2) partial pressure/concentration of CO2
3) saturation of haemoglobin with O2
How does high partial pressure of O2 affect O2 and haemoglobin binding?
if partial pressure of O2 is high, affinity of haemoglobin for O2 will also be high, so O2 binds tightly to haemoglobin
How does low partial pressure of O2 affect O2 and haemoglobin binding?
if partial pressure of O2 is low, O2 is released
How does high partial pressure of CO2 affect O2 and haemoglobin binding?
if partial pressure of CO2 is high, conditions become acidic causing haemoglobin to change shape, so affinity of haemoglobin for O2 decreases, releasing O2 (this is known as the Bohr effect)
What is the Bohr effect?
when partial pressure of CO2 is high, conditions become acidic causing haemoglobin to change shape, so affinity of haemoglobin for O2 decreases, releasing O2
How does the saturation of haemoglobin with O2 affect O2 and haemoglobin binding?
- hard for 1st O2 molecule to bind
- once it does it changes shape to make it easier for 2nd + 3rd molecules to bind (this is known as positive cooperativity)
- it becomes slightly harder for 4th as low chance of finding a binding site
Label diagram of heart.
Use notes.
What are the 2 chambers of the heart?
atria and ventricles
What is the structure of the atria and how does this relate to its function?
thin-walled + elastic
so they can stretch when filled with blood
What is the structure of the ventricles and how does this relate to its function?
thick muscular walls pump blood under high pressure