Mass transport Flashcards
Describe the structure of haemoglobin
-primary = order of a.a joined by polypeptide bonds
-secondary =alpha helix/beta pleated sheets, held by H bonds
-tertiary = specific 3D structure held by H bonds, disulphide bridges and ionic bonds
-quaternary = 4 polypeptide chains and prosthetic haem group
haemoglobin
-red pigment inside erythrocyte which transports oxygen
-2 alpha and 2 beta polypeptide chains. Each chain is attached to a haem group that can combine with oxygen
-protein made of 4 polypeptide chains
Describe the functions of haemoglobin
-readily associate with oxygen at the surface where gas exchange takes place
-readily disassociate from oxygen at those tissues requiring it
Explain the differences between haemoglobin in different organisms and the reasons for these differences
-affinity (chem attraction) for o2 = how readiy haemoglobin binds to o2. This is controlled by the shape of haemoglobin molecule
-different haemoglobins have different affinities for o2 - different organisms have haemoglobin with different amino acid sequences therefore different tertiary and quaternary structures which affects the affinity for o2
what’s partial pressure
measure of its conc in kPa
Explain what’s meant by loading and uploading of oxygen
-Loading/association of oxygen: the process by which haemoglobin binds with oxygen
-Unloading/dissociation of oxygen: the process by which haemoglobin releases oxygen
associating
o2 and haem bind together
disassociation
haem releases o2
affinity
-high affinity for o2 = take up more o2 easily but releases it less easily
-low affinity for o2 = take up o2 less easily but releases it more easily
Haem
-in each haem group there’s one Fe2+ ion
-each iron can combine with single oxygen molecule
-a single haemoglobin molecule therefore can carry 4 oxygen molecules
Describe and explain the shape of oxyhaemoglobin disassociation curve
-in low pp haemoglobin has a low affinity for o2 (disassociates o2 more easily), the curve is shallow
-curve becomes steeper as the affinity for oxygen increases
-curve levels off at nearly 100% saturation at high pp of oxygen - haemoglobin has high affinity for o2 (disassociates less easily)
Explain how the binding of oxygen affects the shape of haemoglobin
-hard for o2 to bind as haem group are in the middle of the haemoglobin molecule
-first o2 causes a conformational change in the haemoglobin (change in shape) making it easier for the second and third molecule to bind
-harder to reach final binding site so fourth oxygen binds less easily
Explain how the properties of the haemoglobin in different organisms relate to their environment and way of life of the organism concerned
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Comment on the saturation of haemoglobin with oxygen at high partial pressures
Hb is highly saturated
Comment on the saturation of haemoglobin at low partial pressures
Hb has low saturation
Describe and explain the Bohr effect
-Haemoglobin has a reduced affinity for oxygen in the presence of carbon dioxide.
-This means it loads oxygen less readily and unloads more easily. This is called the Bohr effect.
-Dissolved carbon dioxide is acidic and this causes haemoglobin to change shape.
-At gas exchange surfaces there is little carbon dioxide, affinity for oxygen in high, oxygen loads readily.
-At respiring tissues carbon dioxide concentration is high, affinity for oxygen is low, oxygen is readily unloaded.
Explain how, with reference to haemoglobin, animals are adapted to their environment
-An animal that lives in an environment with low partial pressure of oxygen will have haemoglobin with a high affinity for oxygen, the curve is to the left - this allows fully saturated haemoglobin at low partial pressures of oxygen