Transport of Oxygen by Haemoglobin Flashcards
What do we mean by ‘partial pressure’ of oxygen?
concentration of oxygen
What does the oxygen dissociation curve show?
relationship between saturation of haemoglobin with oxygen abd the partial pressure of oxygen
Explain why the gradient of the oxygen dissociation curve is shallow initially
shape of haemoglobin makes it difficult for first oxygen to bind so at low oxygen partial pressures little oxygen binds
Explain why the gradient of the oxygen dissociation curve steepens after the first molecule of oxygen has bound
binding of the first oxygen changes the quaternary structure of haemoglobin making it easier for subsequent oxygen molecules to bind.
What is positive cooperativity?
when the binding of the first molecule makes binding of the second easier. It takes a smaller increase in partial pressure of oxygen to bind the second oxygen compared with the first.
Explain why the gradient of the oxygen dissociation curve flattens off after the thrid oxygen has bound.
with the majority of binding sites occupied it is less likely that a single oxygen molecule will find an empty site to bind to
Where on the oxygen dissociation curve do we find haemoglobin with a greater affinity for oxygen (loads easily, unnloads less easily)
to the left
Where on the oxygen dissociation curve do we find haemoglobin with a lower affinity for oxygen (loads less easily, unnloads easily)
to the right
What happens to haemoglobins affinity for oxygen in the presence of carbon dioxide?
affinity is reduced
What is the bohr effect?
the greater the concentration of carbon dioxide the more readily haemoglobin releases oxygen
Describe the affinity for oxygen of haemoglobin at low carbon dioxide, high oxygen partial pressures (ie in lungs)
high affinity
Describe the affinity for oxygen of haemoglobin at high carbon dioxide, low oxygen partial pressures (ie respiring tissues)
low affinity
Explain how high carbon dioxide reduces the affinity of haemoglobin to oxygen
dissolved carbon dioxide is acidic causing haemoglobin to change shape