3B Mass Transport Flashcards
(108 cards)
What kind of protein is haemoglobin?
- globular
What is haemoglobin?
- an oxygen-carrying pigment found in vast quantities in red blood cells
Describe the structure of red blood cells
- biconcave discs for high SA:V ratio
- no nucleus
- more space for haemoglobin for more oxygen transport
Describe the quaternary structure of haemoglobin
- made up of 4 polypeptide chains (globin proteins)
- made of 2 alpha globins and 2 beta globins
- each globin has a prosthetic haem group
How are the 4 globin subunits held together and arranged in haemoglobin?
- held together by disulphide bonds
- arranged with hydrophobic R groups facing inwards which preserves the 3D spherical shape
Why does the hydrophilic R groups facing outwards in haemoglobin benefit the molecule?
- it maintains solubility
Why is the arrangement of the R groups within haemoglobin important for its function?
- if changes occur to amino acid sequence, the function of the protein can change
- eg. in sickle cell anaemia, valine (non-polar) replaces glutamic acid (polar) which affects solubility of haemoglobin (lessens it)
Describe the importance of the prosthetic haem groups in haemoglobin
- prosthetic haem group contains an iron (II) ion (Fe2+) which is able to reversibly combine with an oxygen molecule
- this forms oxyhaemoglobin
- the presence if this causes blood to appear bright red in colour
How many oxygen molecules can each haemoglobin molecule carry?
- 4
- each haem group can carry one molecule
Are all haemoglobin molecules the same?
- the haem group is the same for all types of haemoglobin
- the globin chains can differ lots from different species of haemoglobins
Describe the function of haemoglobin
- responsible for binding oxygen in the lung and transporting oxygen to the tissue to be used in aerobic metabolic pathways (respiration)
How does haemoglobin help with transport of oxygen?
- oxygen isn’t very soluble in water
- haemoglobin is soluble in water
- oxygen can be carried more efficiently around the body when bound to haemoglobin
What does the presence of the haem group enable?
- enables small molecules like oxygen to be bound more easily because as each oxygen binds the quaternary structure is altered
- this is due to changes in the teriary structure
- this causes haemoglobin to have a higher affinity for subsequent oxygen molecules
Describe cooperative binding of haemoglobin
- binding of first oxygen molecule results in a conformational change in the structure of the haemoglobin molecule
- this makes it easier for each successive oxygen molecule to bind
What does the existence of the iron (II) ion in the prosthetic haem group allow?
- allows oxygen to reversibly bind to form oxyhaemoglobin
Which oxygen is hardest to dissociate from the haemoglobin?
- the last one
Describe what partial pressure is
- the pressure of the gas if the gas were in the same volume and temperature by itself
- it can change with altitude
Does altitude affect % composition of a mixture of gases?
no
What does the oxygen dissociation curve describe?
- the relationship between the partial pressure of oxygen and the % saturation of haemoglobin with oxygen
Why can haemoglobin pick up lots of oxygen in the lungs?
- low CO2 in lungs so haemoglobin can pick up more oxygen
- also a high partial pressure of oxygen in the lungs
Why is oxygen dropped off by haemoglobin in respiring tissues?
- the partial pressure of oxygen is low
- the oxygen diffuses out into the body cells down a conc grad
Why can a small change in partial pressure of oxygen have a very large effect on the % saturation of haemoglobin with oxygen?
- because haemoglobin has such a high affinity for oxygen
How does the partial pressure of oxygen in different areas of the body help with transport of oxygen?
- it ensures oxygen is picked up from where there is lots of it and dropped off to where there is less of it
How does pH alter haemoglobin?
- CO2 makes blood more acidic
- pH alters the hydrogen bonds in haemoglobin