Lesson 3.3.4.1.2
3.3.4.1.2 Haemoglobin and oxygen transport Quiz: AQA Biology, Unit 3
20 questions
In partnership with Revision Ninja
Lesson 3.3.4.1.2, Haemoglobin and oxygen transport: 20 multiple choice questions for the AQA Biology (7402), Unit 3: Organisms exchange substances with their environment, written with Revision Ninja.
Host it live on the board and students join with a game code on their own devices, or revise alone with Free Play. The answers are revealed in the game.
The 20 questions
-
What is the quaternary structure of haemoglobin?
- Four polypeptide chains, each with a haem group that binds one oxygen molecule.
- A single polypeptide chain folded into a globular shape with no prosthetic group.
- A long, unbranched chain of amino acids with a glycosidic bond at each binding site.
- Two polypeptide chains joined by disulfide bridges, with a haem group on each chain.
-
What is the Bohr effect?
- An increase in carbon dioxide concentration reduces the affinity of haemoglobin for oxygen, shifting the dissociation curve right.
- A rise in the pH of the blood causes haemoglobin to lose its quaternary structure and stop binding oxygen.
- A fall in temperature causes haemoglobin to release all its oxygen immediately into the blood plasma.
- An increase in carbon dioxide concentration increases the affinity of haemoglobin for oxygen, shifting the curve left.
-
Why does the oxyhaemoglobin dissociation curve have a sigmoid shape?
- The binding of the first oxygen changes the shape of haemoglobin, making the binding of further oxygen molecules easier.
- Oxygen binds to each haem group independently with the same affinity, giving a straight line.
- The binding of the first oxygen blocks further binding sites, so each following oxygen binds more slowly.
- Haemoglobin contains a single binding site, so the curve rises in a straight line to full saturation.
-
Which statement describes the loading of oxygen at the lungs?
- Haemoglobin releases oxygen at the lungs because the carbon dioxide concentration is low there.
- Haemoglobin is unaffected by oxygen partial pressure, so loading depends only on the heart rate.
- Haemoglobin has a low affinity for oxygen, so it becomes unsaturated in the lungs.
- Haemoglobin has a high affinity for oxygen, so it becomes almost fully saturated in the lungs.
-
Which statement describes the unloading of oxygen in respiring muscle tissue?
- Haemoglobin is destroyed by the muscle tissue, so the oxygen is released into the cytoplasm.
- Carbon dioxide and a lower oxygen partial pressure cause haemoglobin to release oxygen to the tissue.
- Haemoglobin releases oxygen only when the pH of the blood is above 8, which is rare in tissues.
- Haemoglobin binds more oxygen because the carbon dioxide concentration in the muscle is high.
-
Many animals have haemoglobins with different oxygen transport properties. Which adaptation does this reflect?
- Animals in low-oxygen environments often have haemoglobins with a higher affinity for oxygen.
- Animals in all environments have identical haemoglobin, so oxygen transport is the same for all.
- Animals in low-oxygen environments always have haemoglobin with a lower affinity for oxygen.
- Animals in low-oxygen environments have no haemoglobin, because it is produced only at high oxygen levels.
-
A haemoglobin solution has a saturation of 60 percent at a partial pressure of oxygen of 4 kPa. What does this tell us about the solution?
- At this partial pressure, 60 percent of the red blood cells have lost their haemoglobin entirely.
- At this partial pressure, 60 percent of the haemoglobin binding sites carry oxygen.
- At this partial pressure, 40 percent of the haemoglobin molecules have broken down into polypeptides.
- At this partial pressure, 60 percent of the oxygen in the solution is dissolved in the plasma.
-
Why is the Bohr effect important in an exercising muscle?
- It increases the binding of oxygen to haemoglobin in the muscle, which blocks respiration.
- It converts carbon dioxide into oxygen so that the muscle can respire aerobically.
- It stops the release of oxygen to the muscle, so that the muscle conserves its energy supply.
- It increases the release of oxygen to the muscle where carbon dioxide production is high.
-
A researcher finds that the dissociation curve of an animal's haemoglobin lies to the left of human haemoglobin. What does this indicate?
- The animal's haemoglobin has a lower affinity for oxygen at a given partial pressure.
- The animal's haemoglobin cannot bind oxygen at any partial pressure in the environment.
- The animal's haemoglobin is identical to human haemoglobin in every oxygen transport property.
- The animal's haemoglobin has a higher affinity for oxygen at a given partial pressure.
-
What is the role of red blood cells in oxygen transport?
- They contain haemoglobin, which binds oxygen in the lungs and releases it in the tissues.
- They contain xylem vessels, which carry oxygen from the lungs to the tissues by mass flow.
- They contain phloem, which carries oxygen dissolved in sugar solutions to the heart.
- They contain myoglobin, which binds oxygen in the plasma and carries it to the lungs.
-
Which statement about the affinity of fetal haemoglobin for oxygen is consistent with its role?
- Fetal haemoglobin has a higher affinity for oxygen, so oxygen can move from maternal blood to the fetus.
- Fetal haemoglobin has a lower affinity for oxygen, so the fetus receives less oxygen from the mother.
- Fetal haemoglobin is identical to adult haemoglobin, so it provides no advantage for oxygen transfer.
- Fetal haemoglobin has no affinity for oxygen, so the fetus relies entirely on carbon dioxide transport.
-
A student states that the oxygen dissociation curve shows haemoglobin binding oxygen at a constant rate. Which evaluation is correct?
- The claim is partly correct, because binding is constant only in the presence of carbon dioxide.
- The claim is correct, because haemoglobin binds oxygen at the same rate regardless of partial pressure.
- The claim is wrong, because binding is cooperative, so the rate changes as more oxygen binds.
- The claim is correct, because the sigmoid curve shows a constant gradient across the whole range.
-
Which pigment is found in muscle tissue and has a higher affinity for oxygen than haemoglobin?
- Myoglobin
- Chlorophyll
- Melanin
- Carotene
-
A person's blood has a low concentration of haemoglobin. What is the most likely effect on oxygen transport?
- Less oxygen can be carried in the blood, so tissues may receive less oxygen for respiration.
- Oxygen is carried entirely in the plasma, so haemoglobin concentration has no effect.
- More oxygen is carried in the blood, because each haemoglobin molecule binds more oxygen.
- The person's dissociation curve shifts to the right, so they absorb more oxygen at the lungs.
-
Which of these is the correct sequence for the loading and unloading of oxygen by haemoglobin?
- Loading and unloading both occur at the heart, which pumps oxygen to the lungs and tissues.
- Loading at the tissues where oxygen partial pressure is low, then unloading at the lungs.
- Loading and unloading both occur at the lungs, which controls the oxygen supply to all tissues.
- Loading at the lungs where oxygen partial pressure is high, then unloading at tissues where it is low.
-
A rise in temperature during exercise shifts the dissociation curve to the right. What is the effect on oxygen delivery?
- Oxygen delivery is unchanged, because temperature has no effect on the affinity of haemoglobin.
- Oxygen is released into the lungs, so the blood becomes depleted of oxygen before reaching the muscles.
- Oxygen is released more readily to the working muscles, which helps to meet their demand.
- Oxygen is bound more tightly to haemoglobin, so less oxygen is available to the muscles.
-
In the lungs the oxygen partial pressure is high, and in a resting tissue it is lower. Which statement describes haemoglobin in the tissue?
- It has a higher saturation in the tissue than in the lungs, so it stores oxygen in the tissue.
- It releases oxygen in the lungs and binds oxygen in the tissue, which reverses the normal sequence.
- It has a lower saturation in the tissue than in the lungs, so it releases oxygen to the tissue.
- It has the same saturation at both sites, because oxygen partial pressure has no effect on binding.
-
Which of these changes would shift the oxyhaemoglobin dissociation curve to the right?
- A decrease in temperature of the blood at the tissue.
- A rise in the pH of the blood as it passes through the lungs.
- A decrease in carbon dioxide concentration in the blood.
- An increase in carbon dioxide concentration in the blood.
-
A student claims that haemoglobin is the best oxygen carrier for all animals. Evaluate this claim.
- The claim is accurate, because haemoglobin is identical in every animal species that has been studied.
- The claim is too strong, because animals have different haemoglobins adapted to their own environments.
- The claim is accurate, because myoglobin carries less oxygen than haemoglobin in every animal tissue.
- The claim is wrong, because haemoglobin carries no oxygen at all and only binds carbon dioxide.
-
Why does myoglobin store oxygen in muscle more effectively than haemoglobin would?
- It has a higher affinity for oxygen, so it binds oxygen even at the low partial pressures found in muscle.
- It has a lower affinity than haemoglobin, so it releases oxygen more readily into the blood plasma.
- It carries carbon dioxide away from the muscle, which frees its oxygen binding sites for storage.
- It is found only in red blood cells, which store oxygen for the whole body at all times.
Related quizzes
- Surface area to volume ratio and exchange Quiz · 3.3.1.1 · 20 questions
- Gas exchange surfaces and their adaptations Quiz · 3.3.2.1 · 20 questions
- Gas exchange in the human gas exchange system Quiz · 3.3.2.2 · 20 questions
- Digestion and absorption of food Quiz · 3.3.3.1 · 20 questions
- Circulatory system, arteries, veins and capillaries Quiz · 3.3.4.1.1 · 20 questions
- Mass transport in plant tissues Quiz · 3.3.4.2.1 · 20 questions
- Monomers, polymers, condensation and hydrolysis Quiz · 3.1.1.1 · 20 questions
- Eukaryotic cell structure and organelles Quiz · 3.2.1.1.1 · 20 questions
- DNA, genes, loci and chromosomes Quiz · 3.4.1.1 · 20 questions
- Light-dependent and light-independent reactions Quiz · 3.5.1.1 · 20 questions