7.Mass Transport Flashcards
What is the structure of haemoglobin
Primary-sequence of amino acids in the four polypeptides
Second-each polypeptide coiled into a helix
Tertiary-each polypeptide folded into precise shape -important
Quarte-all 4 linked together to form spherical molecule, each polypeptide associated with haem group contains a ferrous ion
What does the ferrous ion in the haem group do
Each one can combine with single oxygen molecule, so 4 oxygen molecules carried by one haemoglobin molecule in humans
What is unloading and loading oxygen
Process by which haemoglobin binds with oxygen is loading or associating.
Process by which haemoglobin releases its oxygen is unloading or dissociating
Haemolglon with a high affinity for oxygen, take up more easily but release less easily and haemoglobin with low affinity for oxygen, take up oxygen ,es easily but release more easily
To be efficient at transporting oxygen haemglobin must:
Readily associate with oxygen at surface of gas exchange
Readily dissociate from oxygen at tissues requiring it
How does haemoglobin achieve both properties
- changes affinity under different conditions
- shape changes in presence of certain substances eg carbon dioxide
- new shape haemoglobin molecule binds more loosely to oxygen as result it releases it oxygen
What’s the oxygen dissociation curve
Graph showing the relationship between the saturation of haemoglobin with oxygen and the partial pressure of oxygen
How to understand different oxygen dissociation curves on the graph
Further to the left-greater the affinity of haemoglobin (loads readily but unloads less easily)
Further to right-lower affinity of haemoglobin (loads less readily )
Explanation of the oxygen dissociation curve
1-shape of haemoglobin means hard for first oxygen to bind, low oxygen conc little oxygen binds, gradient of curve is shallow
2-binding of first oxygen changes shape of haemoglobin, easier for next two oxygen molecules to bind to other subunits
3-therefore smaller increase in partial pressure needed to bind second oxygen than first one, positive cooperativity gradient steepens
4-after binding of 3rd harder to bind fourth as probability of finding empty subunit is less likely, gradient levels off
What’s the Bohr effect
The greater the conc of carbon dioxide the more readily haemoglobin releases its oxygen.
Why does the conc of carbon dioxide change shape of haemoglobin
Dissolved carbon dioxide is acidic and the low pH causes haemoglobin to change shape
What are features of transport systems
- suitable medium for carrying materials, liquid base on water as dissolves substances and can be breathed as gas
- form of mass transport, moved around in bulk more rapid than diffusion
- closed system of tubular vessels, branching network throughout organism
- mechanism for moving transport medium, requires pressure difference between one part and another
How is mechanism of mass transport achieved
1-use muscular contraction of body muscle or of a specialised pumping organ eg heart
2-rely on natural passive processes eg evaporation of water
What is a double closed circulatory system
Blood is confined to vessels and passes twice through the heart in each complete circuit of the body
Because when passed through lungs pressure reduced
What are the two sections of the heart and the differences between them
Atrium - thin walled and elastic and stretches as collect blood
Ventricle - thicker muscular wall as it has to contract strongly to pump blood some distance
Where does blood from left and right ventricle go to?
Left- goes to body
Right - goes to lungs (thinner muscular wall)
Where are the bicuspid valves
Between atrium and ventricles
Called atrioventricular valves
Where does the aorta connect to
Left ventricle and carries oxygenated blood around body