Chapter 7 Flashcards
What makes up haemoglobin?
4 polypeptide chains and 4 prosthetic haem groups
Haemoglobin primary structure
4 polypeptide chains
Secondary structure of haemoglobin
Each polypeptide is coiled in a helix
Haemoglobin tertiary structure
Each polypeptide is folded into specific shapes
Haemoglobin quaternary structure
Four polypeptides are associated with a haem group
Affinity definition
Is the ease at which haemoglobin binds to O2
The role of haemoglobin (3 things)
To transport O2, to increase the efficiency of O2 transport, haemoglobin must readily associate and dissociate O2
On a dissociation curve if the curve is further to left what does this say about the affinity?
Curve further to left, the greater the affinity
With oxygen dissociation, the higher the pH the what the affinity
Higher
With oxygen dissociation, the higher the [CO2] the what the affinity
Lower
Mass transport defintion
Moving substances efficiently over large distances
Structure of arteries
Thick elastic walls and smooth muscle, quite a narrow lumen
Structure of arterioles
Smaller arteries - thinner elastic walls and less smooth muscle
Structure of a vein
Thin walls with a much larger lumen, has valves
Mass flow theory
Active transport is used to actively load the solutes into the sieve tubes of the phloem at the source
This lowers the water potential inside the sieve tubes, so water enters the tubes by osmosis from the xylem
This creates a high pressure inside the sieve tubes at the source end of the phloem
At the sink end, solutes are removed from the phloem
This increases the water potential inside the sieve tubes, so water re enters the xylem by osmosis
This lowers the pressure inside the phloem at the sink end
The result is a pressure gradient from the source end to the sink end
This gradient pushes solutes along the phloem to the sink - where they are needed