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Module: BIOM - 1006

Lecturer: Dr Rushworth

Date: 25/10/16

Haemoglobin and Myoglobin
o

Haemoglobin is one of 2 oxygen-binding proteins found in all vertebrates
 The function of this protein is to carry oxygen from the lungs to other tissues in the body and
deposits it with myoglobin, the other oxygen-binding protein
 Haemoglobin is found within the erythrocytes (red blood cells)
 In mammals, haemoglobin makes up 96% of the dry weight of an erythrocyte
 This suggests that a red blood cell is nothing more than a sack for carrying haemoglobin as
mature erythrocytes do not have any internal organelles
 Haemoglobin has an oxygen-binding capacity of 1
...

In metabolically active tissue, the concentrations of these are very high and so, shift the
dissociation curve to the right, making it easier for oxygen to release
 This is known as the Bohr effect
 This occurs because there are H+ binding sites on the molecule that have a higher
affinity for binding H+ in deoxyhaemoglobin than oxyhaemoglobin

o

Myoglobin, the other oxygen-binding protein is very abundant in tissue where much aerobic
respiration takes place, such as skeletal muscle tissue and cardiac tissue
 It consists of only one polypeptide chain of 153 amino acids
 It is very small and only has a molecular mass of 17
...
These are very important as:
 They stop the possibility of the haem groups of 2 neighboring
haemoglobin molecules coming into contact with each other and
oxidising the Fe2+
 It also stops CO binding with the most efficient configuration of
Fe2+, therefore lowering the affinity of CO to the haemoglobin
molecule
 This is very important, as when CO binds to haemoglobin, it
cannot release it, therefore it can no longer bind to
oxygen



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