Transporting oxygen and carbon dioxide Flashcards
What is the structure of haemoglobin
Large globular protein made up of 4 peptide chains each with an iron containing prosthetic group
How does oxyhameoglobin form
molecule formed when oxygen binds to haemoglobin
What is the equation to from oxyhaemglobin
Hb + 402 =Hb4O2
What happens when the first oxygen molecule that binds to the haemoglobin (disscoation curve)
It alters the arrangement of the molecule making it easier for the following oxygen molecules to bind
What is the structure of haemoglobin
Quaternary structure
What does this mean “affinity of hameglobin for oxygen”
The ability of haemglobin to attract, or bind oxygen
What does this mean
“Saturation of hameglobin with oxygen”
When hameglboin is holding the maximum amount of oxygen it can bind
What is “loading/ association of hameglobin”
The binding of oxygen to haemglobin
What does this mean “Unloading/ dissociation of haemoglobin”
When oxygen detaches, or unbinds from haemoglobin
What happens when we have lower partial pressure of oxygen
`Haemoglobin does not have a high affinity this causes the Haemoglobin to unload oxygen in those regions
Why is it an advantage that haemoglobin is unloading at low partial pressure
It means the haemoglobin is unloading oxygen at site where the oxygen is needed
What happens when theris lots partial pressure
It has a high affinity for oxygen so it will be loading or associating lots of oxygen
What is the Bohr effect
Changes in the oxygen dissociation curve of haemoglobin that occur due to a rise in carbon dioxide levels and a reduction of affinity of haemoglobin for oxygen
What happens when the bhor effect takes place
as the proportion of CO2 rises, the hameglobin curve moves down and to the right
If the curve shifts left what does that tell us
increased affinity and therefore uploads more oxygen
if the curve shifts right what does that tell us
decreased affinity and there for unloads more oxygen
How is fetal haemoglobin different to adult haemoglobin
Higher affinity for oxygen even at that same partial pressure of oxygen
What is myoglobin
respiratory pigment found in the muscle tissue of vertebrates with a higher affinity for oxygen than haemoglobin
What are some similarities between haemoglobin and myoglobin
Both are oxygen carrying pigments composed of heme proteins and iron.
Both proteins are capable of increasing the amount of dissolved oxygen in biological fluids of vertebrates as well as in some invertebrates.
What are differences between structure in haemoglobin and myglobin
Quaternary structure in hameglobin
and a monomer and lacks Quaternary structure in myoglobin
Diffrences in polypeptide chains in hameglobin and myoglonin
Hemoglboin has 4 PP chains
Myoglobin has single PP chain
Oxygen binding ability between hameoglobin and myglobin
Hemoglboin has a low affinity to bind with oxygen
Myoglobin has a high afiinity to bind with oxygen which does not depend on the oxygen concentration
How does mylgobin act as storage molecule
when oxygen binds to myglobin it does not give it up very easily
When does myoglobin release oxygen
when the oxygen levels in very active muscle tissue get really low the CO2 levels are high myoglobin release its store of oxygen
What causes the Bhor affect
presence of co2 is caused by the acidic nature of dissolved co2
