4- transport of gases in blood Flashcards
(12 cards)
1
Q
structure of haemoglobin
A
- composed of four polypeptide chains: two alpha chains and two beta chains
- each chain has a haem group with an iron atom, which can bind to one molecule of oxygen
- one haemoglobin molecule can carry up to four oxygen molecules
2
Q
role of haemoglobin in gas exchange
A
- haemoglobin transports O2 from the lungs to tissues and CO2 from tissues to the lungs
- oxygen transport: oxygen binds to the iron in the haem groups, forming oxyhaemoglobin
- carbon dioxide transport: some carbon dioxide is carried in the bloodstream bound to haemoglobin (carbaminohaemoglobin)
3
Q
Bohr affect on haemoglobin
A
- the effect of pH on the oxygen- binding affinity of haemoglobin
- high pH (low carbon dioxide concentration): leads to a higher affinity for oxygen, facilitating oxygen uptake in the lungs
- low pH (high carbon dioxide concentration): leads to a lower affinity for oxygen, facilitating oxygen release in respiring tissues
4
Q
oxygen dissociation curve
A
- a graph showing the relationship between oxygen pressure (PO2) and the oxygen- carrying capacity of haemoglobin
- sigmoidal shape: indicates that as the oxygen pressure increases, more oxygen binds to haemoglobin until it becomes fully saturated
- left shift: occurs at higher pH levels, lower temperatures, or lower carbon dioxide levels- this signifies a higher affinity of haemoglobin for oxygen
- right shift (bohr effect): occurs at lower pH levels, higher temperature, or higher carbon dioxide levels, this signifies a lower affinity of haemoglobin for oxygen
5
Q
myoglobin structure
A
- single polypeptide chain with 153 amino acids
- contain one heme (iron containing) group
6
Q
function of myoglobin
A
- stores oxygen in muscle cells, releasing it during periods of hypoxia or intense exercise
7
Q
myoglobin vs haemoglobin
A
- haemoglobin is a tetramer, with four polypeptide subunits. myoglobin is monomeric
- haemoglobin transports oxygen in the blood from the lungs to the tissues. myoglobin stores oxygen in muscle cells
8
Q
myoglobin oxygen affinity
A
myoglobin has higher oxygen affinity than adult haemoglobin, to store oxygen effectively
9
Q
structure of foetal haemoglobin
A
- composed of two alpha and two gamma chains
- contains two heme groups
10
Q
function of foetal haemoglobin
A
transports oxygen from mothers bloodstream to the foetus
11
Q
foetal haemoglobin vs adult haemoglobin
A
- adult haemoglobin is made up of two alpha and two beta chains. foetal haemoglobin has two alpha and two gamma chains
- foetal haemoglobin has a higher oxygen affinity than adult haemoglobin, facilitating effective oxygen transfer from mother to foetus
12
Q
oxygen affinity in foetal haemoglobin
A
higher than adult haemoglobin, to effectively extract oxygen from the mothers blood