Mass transport in animals Flashcards
(64 cards)
What are haemoglobin?
Proteins with a quaternary structures, different forms are found in different organisms
What is the role of heamoglobin
- They unload oxygen under a set of conditions and they load oxygen under a set of conditions
- Bind to oxygen in order to transport it across the body
Describe the primary structure of heamoglobin molecules
Sequences of amino acids in 4 polypeptide chains
Describe the secondary structure of haemoglobin molecules
Each of the 4 polypeptide chains twist to form an alpha helix structure
Describe the tertiary structure of haemoglobin molecules
Each polypeptide chain is folded into a specific shape, important for the role of carrying oxygen
Describe the quaternary structure of haemoglobin molecules
4 polypeptide chains are linked to form a spherical molecule
Each polypeptide is associated with a haem group, which has an FE2+ ion
Each FE2+ ion can combine with a single O2 molecule, meaning there is a total of 4 O2 molecules that can be carried by a single heamoglobin molecule in humans
A and B link to form a spherical molecule
What is meant by loading/ assosciation of oxygen molecules
This is the process of haemoglobin binding to oxygen molecules, this happens in the lungs
What is meant by unloading/ disassociation of oxygen molecules
This is the process of haemoglobin releasing its oxygen molecules, this happens in the tissues
What is haemoglobins role which makes it efficient at transporting oxygen
Readily associates with oxygen at the surface where gas exchange takes place
Readily dissociates with oxygen at tissues requiring
Describe the affinity of haemoglobin
Haemoglobin can change its affinity for oxygen under certain conditions
This is because the haemoglobins shape changes in certain substances such as carbon dioxide
CO2 causes the shape of the haemoglobin to change so it binds more loosley to oxygen, causing it to release its oxygen
Explain how affinity of haemoglobin changes around the body
At a gas exchange surface, oxygen concentration is high, and CO2 concentration is low, causing haemoglobin to have a higher affinity meaning oxygen associated
At a respiring tissue, oxygen concentration is low and CO2 concentration is high, causing haemoglobin to have a lower affinity so oxygen is dissociated
Explain how DNA leads to different heamoglobin molecules having different affinities for oxygen
Different base sequences in DNA/ amino acid sequences/ teritary structure/ different quatenary shape and structure means there are different affinities for oxygen
Why might someone breathing in CO cause unconsiousness
-CO begins to occupy all sites on haemoglobin instead of oxygen,
- This means no oxygen will be carried to respiring tissues, respiration reduces, less function of tissues
Describe what an oxygen dissociation curve shows
- Graph of the relationship between the saturation of the haemoglobin with oxygen and the partial pressure of oxygen
Explain the shape of the oxygen dissociation curve
- The shape of the haemoglobin makes it hard for the first oxygen molecule to bind to one of the sites on one of its 4 polypeptide subunits as they are close together, this means at low oxygen conc, there is a little oxygen binding to the haemoglobin molecule
- The binding of this first oxygen molecule causes the quatenary structure and therefore the shape of it to change, making it easier for the other sub-units to bind to the oxygen molecule,
-This means there is a smaller increase of partial pressure needed to bind the second oxygen than the first ( positive cooperativity) this means gradient of the graph steepens
This changes after the binding of the 3rd oxygen, in practise it is harder to bind the 4th oxygen molecule due to probability as most binding sites are occupied, harder to find a free binding site for 4th oxygen molecule
Gradient of the graph reduces and graph flattens off
Describe 2 features of the oxygen dissociation curve that structure the curve
-Further to the left of the curve, greater affinity of haemoglobin for oxygen, loads easier but unloads less easily
- Further to the right of the curve haemoglobin has a lower affinity for oxygen, unloads easier but loads less easy
Define partial pressure
The amount of a gas that is present in a mixture is measured by its contribution of pressure to the overall pressure
Measured in kPa
Describe how haemoglobin may behave at a gas exchange surface and how this influences an oxygen dissociation curve
Gas exchange surfaces have low concentrations of CO2 because it diffuses across exchange surface in order to be excreted , this means haemoglobin has a higher affinity for oxygen, coupled with the high concentration of oxygen in the lungs, means that oxygen is readily loaded by haemoglobin
This means a graph plotted using figures from blood at a gas exchange surface will shift the graph left due to low CO2 conc
Describe how haemoglobin may behave differently at a highly respiring tissue and how does this influence an oxygen dissociation curve
Respiring tissues have high concentrations of CO2 , meaning affinity of haemoglobin in this area is reduced, coupled with the low concentration of oxygen in the muscles, means that oxygen is readily unloaded from haemoglobin into muscle cells
This means a graph plotted using figures from blood at respiring tissues will shift right, due to high conc of CO2
Describe the loading, transport and unloading
Loading- at a gas exchange surface carbon dioxide is always being removed, meaning there is a low conc of CO2 here, causing PH to slightly increase, changing the shape of haemoglobin enabling it to load oxygen readily
Transport- New shape of haemoglobin due to increased PH means that affinity is increased so oxygen is not released during transportation
Unloading- Carbon dioxide is released by respiring tissues, and CO2 is acidic in solution meaning shape of haemoglobin is changed to have a lower affinity of oxygen causing haemoglobin to unload its oxygen
How do the adaptions of haemoglobin ensure sufficient oxygen is being transported to active tissues?
Higher rate of respiration in tissues means there is more CO2 produced, lowering the PH, meaning the greater the shape of the haemoglobin changes meaning the more readily the oxygen is unloaded so it is more avainable for respiration
Describe common features of exchange systems
- A suitable medium in which to carry substances e.g blood usually liquid based as water can dissolve substances and move easily but this can also be gases
-Form of mass transport, bulk over large distances
-Closed system of tubular vessels containing transport medium and forms branching network to distrubute to all areas of the body
-Mechanism for moving transport medium, needs a pressure gradient
Describe the circulatory system of mammals
Double closed circulatory system
where blood is confined to vessels and passes through the heart twice for each complete circuit
This is because when blood passes through the lungs pressure decreases, if this passed immediately to the body low pressure would make circulation very slow
Blood is then returned to the heart to increase the pressure before being circulated to the rest of the tissues
High temp and metabolism in body is therefore needed as substances are delivered around the body quickly
Arteries veins and cappilaries are used, diffusion at the end large SA, short pathway, steep siffusion gradient
Describe function of renal vein
Carries deoxy blood away from the kidney