B7 Flashcards
(94 cards)
what are haemoglobins
protein molecules with a quaternary structure that makes it efficient at loading oxygen in one set of conditions and unloading it in another
structure of haemoglobin
primary, secondary, tertiary, quaternary
- globular protein
- hydrophillic side chains face outwards
–> haemoglobin = soluble so good for transport - 2 pairs of polypeptides
- linked to form a spherical molecule
–> 2 pairs: 4 chains. 2 a-helices, 2 B-pleated sheets. - conjugated protein- w prosthetic groups (haem)
primary
sequence of amino acids in the 4 polypeptide chains
secondary
each chain = coiled due yo hydrogen bonding
tertiary
each chain = folded in precise shape– important in its ability to carry oxygem
quaternary
all 4 polypeptides = linked to form almost spherical molecule
- hydrogen, ionic, disulfide, hydrophobic
each polypeptide = associated with a haem group, which contain a ferrous Fe2+ ion
- each Fe2+ ion can combine with a single O2 molecule, so 4 O2 molecules can be carried per hb molecule in humans
loading/ associating
the process by which hb binds with O2
takes place in lungs
unloading/ dissociating
the process by which hb releases its O2
hb with high O2 affinity…
- load easily
- unload less easily
hb with low O2 affinity…
- unload easily
- load less easi;y
the role of haemoglobin
- how it is efficient
role: to transport O2
to be efficient:
- readily associate w O2 at gas exchange surface
- readily dissociate w O2 at tissues requiring it
hb changes its affinity for O2 under different conditions
- its shape changes in the presence of certain substances e.g. CO2
–> in the presence of CO2, the new hb shape binds more loosely to O2 so it releases its O2
gas exchage surface
- oxygen conc
- carbon dioxide conc
- affinity of hb for O2
- result
high
low
high
o2 = associated
respiring tissues
- oxygen conc
- carbon dioxide conc
- affinity of hb for O2
- result
low
high
low
o2 = dissociated
why are there different haemoglobins
+
why do different hb have different affinities for O2
- different organisms require hb to more/less readily associate with o2 at different partial pressures
- different haemoglobins have different shaped molecule
- each species produces hb with a slightly different amino acid sequence
- the hb therefore has slighty different tertiary/quaternary structures
–> hence different O2 binding properties
hb conditions
partial pressure of O2 =
pH =
O2 concentration
CO2 concentration
change in structure of hb –> change in affinity for oxygen
- what are the two ways this change in structure occurs
- different types of hb have diff tertiary structure
- the same hb can change its structure and so its own affinity for O2 in diff environmental conditions
what is the oxygen dissociation curve
explanation of the shape of oxygen dissociation curves
when hb is exposed to different partial pressures of O2, it does not bind to the O2 evenly
the graph of the relationship between the saturation of hb with oxygen and the partial pressure of O2
- ‘tense’ state
- the shape of the hb molecule makes it difficult for the 1st O2 molecule to bind to one of the sites of its 4 polypeptides as they are closely united
—> so at low concentrations, little O2 binds to hb
the gradient of the curve = initially shallow
2+3. conformational change of quaternary structure
- the binding of the 1st O2 molecule changes the quaternary structure of the hb
- this makes it easier for other subunits to bind to O2
—> it therefore takes a smaller increase in the partial pressure of O2 to bind the 2nd O2 compared to the 1st
—> known as POSITIVE COOPERATIVITY
- after the 3rd O2 molecule, binding 4th = harder
—> due to probability
majority of binding sites = occupied, so less likely that a single O2 molecule will find an empty site to bind to
—> graph flattens off
how does the CO2 concentration affect hb’s affinity for O2
hb has reduced affinity for O2 in the presence of CO2
the greater the concentration of CO2, the more readily the hb releases its O2
= THE BOHR EFFECT
why does the behaviour of hb change in different regions of the body
- gas exchange surface
- rapidly respiring tissues
gas exchange surface
- e.g. lungs
- low CO2 conc as it diffuses across the exchange surfaces and is excreted from the organism
- the affinity of hb for O2 is increased
–> coupled with a high O2 conc in the lungs
so O2 is readily loaded by hb
* the reduced CO2 conc shifts the oxygen dissociation curve to the left
rapidly respiring tissues
- e.g. muscles
- high CO2 conc
- affinity of hb for O2 is reduced
—> coupled with low conc of O2 in muscles
so O2 is readily unloaded by hb
* the increased CO2 conc shifts the oxygen dissociation curve to the right
why does greater CO2 conc lead to hb unloading O2
dissolved CO2 = acidic
the low pH causes hb’s tertiary structure to change
the process of loading, transporting, unloading O2
- at the gas exchange surface, CO2 = constantly being removed
- the pH is slightly raised due to low conc of CO2
- the higher pH changes the shape of hb into one that enables it to load O2 readily
- this shape also increases the affinity of hb for O2, so it is not released when being transported in blood to tissues
- in tissues, CO2 = produced by respiring cells
- CO2 = acidic in solution
- so the pH of the blood within tissues = lowered
- the lower pH changes the shape of the hb to one with a lower affinity for O2
- hb releases its O2 into respiring tissues
the process of loading, transporting, unloading O2 in more active, exercising tissues
the higher the rate of respiration, the more CO2 the tissues produce + LACTIC ACID PRODUCED + HIGHER TEMPERATURE, the lower the pH, the greater the hb changes shape, the more readily the O2 = unloaded, the mored O2 = available for respiration
why is hb’s overall saturation not 100%
what happens when hb reaches a tissue w a low respiratory rate
what happens when hb reaches an active tissue
- in humans, hb usually becomes saturated with O2 as it passes through the lungs
- in practice not all hb molecules are loaded with their maximum 4 O2 molecules
- as a consequence, the overall saturation of hb at atm = around 97%
- when this hb reaches a tissue with a low respiratory rate, only one of these molecules will normally be released
- the blood returning to the lungs will therefore contain hb that is still 75% saturated with O2
- when hb reaches a very active tissue, 3 O2 molecules will usually be unloaded from each hb
why do different species have different types of hb
types of hb have evolved within species as adaptations for different environmental conditions
e.g. a species of animal that lives in an environment with a lower pp of O2 have evolved hb that has a higher affinity for O2
lugworm and hb
- the lugworm is not very active, spending most of its time in a u-shaped burrow
- most of the time the lugworm is covered by sea water, which it circulates through its burrow
- O2 diffuses into the lugworm’s blood from the water and it uses hb to transport O2 to tissues
- when the tide goes out, the lugworm can no longer circulate a fresh supply of oxygenated water through its burrow
- as a result, the water in the burrow contains progressively less O2 as the lugworm uses it up
- the lugworm has to extract as much O2 as possible from the water in the burrow if it is to survive until the tide comes in again
- the O2 dissociation curve of lugworm hb is shifted far to the left than that of humans
–> hb of lugworm = fully loaded even if there is little O2 available
llama and hb
- lives at high altitudes
- at these altitudes, atm = lower so pp of O2 = lower
- it is therefore difficult to load hb with O2
- llamas have a type of O2 that has a higher affinity for O2 than humans- so O2 dissociation = shifted to left
why do large organisms have a transport system
- all organisms exchange materials between themselves and their environment
- in small organisms, this exchange can take place by diffusion over the body surface
- however, increasing in size, the surface area to volume ratio decreases, so the needs of the organism cannot be met by the body surface alone
- specialist exchange surfaces are needed to absorb nutrients and respiratory gases, and remove excretory products
- the exchange surfaces are located in specific regions of the organism
- a transport system is required to take materials from cells to exchange surfaces and vice versa
- materials also need to be transported between different parts of an organism
- as organisms have evolved to be more complex, their tissues and organs have become more specialised and dependent on each other
—> so transport systems = essential
whether or not there is a specialised transport medium, and whether or not is circulated by a pump is dependent on 2 factors:
the surface to volume ratio
the metabolic rate / how active the organism is