Hemoglobin questions with solutions
A gene codes for the α-polypeptide chain. There are 423 bases in this gene that code
for amino acids. How many amino acids are there in the α-polypeptide chain?
✅✅141;
The hemoglobin in one organism may have a different chemical structure from the
haemoglobin in another organism. Describe how. ✅✅Different primary
structure/amino acids/different number
of polypeptide chains;
The graph shows oxygen dissociation curves for horse haemoglobin and for llama
haemoglobin. Horses are adapted to live at sea level and llamas are adapted to live in
high mountains.
Use the graph to explain why llamas are better adapted to live in high mountains than
horses (llama more to the left) ✅✅1. Low partial pressure of oxygen;
2. In lungs;
3. (Llama) haemoglobin able to load more
oxygen/(llama) haemoglobin saturated (at
low/particular partial pressure of oxygen);
4. Higher affinity for oxygen;
The oxygen dissociation curve of the fetus is to the left of that for its mother. Explain
the advantage of this for the fetus. ✅✅1. Higher affinity / loads more oxygen;
2. At low/same/high partial pressure/pO2;
3. Oxygen moves from mother/to fetus;
After birth, fetal haemoglobin is replaced with adult haemoglobin. Use the graph to
suggest the advantage of this to the baby. ✅✅1. Low affinity / oxygen dissociates;
2. (Oxygen) to respiring
tissues/muscles/cells;
Hereditary persistence of fetal haemoglobin (HPFH) is a condition in which production
of fetal haemoglobin continues into adulthood. Adult haemoglobin is also produced.
People with HPFH do not usually show symptoms. Suggest why ✅✅Enough adult
Hb produced / enough oxygen
released / idea that curves/affinities/Hb are
similar / more red blood cells produced;
Lugworms live in mud where the partial pressure of oxygen is low. The graph shows
oxygen dissociation curves for a lugworm and for a human. (lugworm is far to the left
and more steep)
Explain the advantage to the lugworm of having haemoglobin with a dissociation curve
in the position shown. ✅✅High(er) affinity for oxygen /
absorbs/loads more oxygen;
A gene codes for the α-polypeptide chain. There are 423 bases in this gene that code
for amino acids. How many amino acids are there in the α-polypeptide chain?
✅✅141;
The hemoglobin in one organism may have a different chemical structure from the
haemoglobin in another organism. Describe how. ✅✅Different primary
structure/amino acids/different number
of polypeptide chains;
The graph shows oxygen dissociation curves for horse haemoglobin and for llama
haemoglobin. Horses are adapted to live at sea level and llamas are adapted to live in
high mountains.
Use the graph to explain why llamas are better adapted to live in high mountains than
horses (llama more to the left) ✅✅1. Low partial pressure of oxygen;
2. In lungs;
3. (Llama) haemoglobin able to load more
oxygen/(llama) haemoglobin saturated (at
low/particular partial pressure of oxygen);
4. Higher affinity for oxygen;
The oxygen dissociation curve of the fetus is to the left of that for its mother. Explain
the advantage of this for the fetus. ✅✅1. Higher affinity / loads more oxygen;
2. At low/same/high partial pressure/pO2;
3. Oxygen moves from mother/to fetus;
After birth, fetal haemoglobin is replaced with adult haemoglobin. Use the graph to
suggest the advantage of this to the baby. ✅✅1. Low affinity / oxygen dissociates;
2. (Oxygen) to respiring
tissues/muscles/cells;
Hereditary persistence of fetal haemoglobin (HPFH) is a condition in which production
of fetal haemoglobin continues into adulthood. Adult haemoglobin is also produced.
People with HPFH do not usually show symptoms. Suggest why ✅✅Enough adult
Hb produced / enough oxygen
released / idea that curves/affinities/Hb are
similar / more red blood cells produced;
Lugworms live in mud where the partial pressure of oxygen is low. The graph shows
oxygen dissociation curves for a lugworm and for a human. (lugworm is far to the left
and more steep)
Explain the advantage to the lugworm of having haemoglobin with a dissociation curve
in the position shown. ✅✅High(er) affinity for oxygen /
absorbs/loads more oxygen;
