haemoglobin Flashcards
explain cooperative binding
At low partial pressure of oxygen, little increase in saturation as oxygen increases.
- Binding of first oxygen changes tertiary structure
- Uncovering another oxygen binding site.
- rapid rise (in saturation of haemoglobin with oxygen)
as it gets easier for oxygen to bind.
define partial pressure
It is a measure of the concentration of a gas in a mixture of gases or a liquid.
Draw the same dissociation curve on the graph but in the presence of a higher ppCO2
-dissociation curve is to the right of adult curve and S shape due to cooperative binding of oxygen.
to the right as:
-Metabolic reactions in tissues causes increased respiration rate.
Increased CO2 production
Dissolves in blood as carboxylic acid
Causes lowering of blood pH
Increased acidity
Changes haemoglobin tertiary structure
Haemoglobin unloads more oxygen more readily to respiring tissue at the same partial pressure of oxygen.
Describe and explain
how organism A (dissociation curve is to the left) is
adapted for life in lower partial pressures of
oxygen relative to
organism B.
Organism A haemoglobin has a higher affinity for oxygen than B.
associates with oxygen more readily
So becomes more saturated at same partial pressure of O2.
Able to supply enough O2 to tissues
O2 used for aerobic respiration
Prevents anaerobic respiration
Describe and explain
Why haemoglobin type 2 (dissociation curve is to the right ) is an advantage over
type 1 in a disease
where one would need more oxygen?
Haemoglobin type 2 has a lower affinity for oxygen than type 1.
Unloads oxygen more readily
Releasing more oxygen quicker to tissues
Oxygen used for aerobic respiration
Allowing greater respiration rate meeting demand for ATP.
bohr effect
a high co2 concentration causes oxyhaemoglobin curve to shift to the right
affinity for o2 decreases as the acidic co2 changes the shape of haemoglobin slightly
