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Question: Regarding haemoglobin molecule
- Haemoglobin is an allosteric protein consisting of four pairs of globin chains
- Fetal haemoglobin has gamma chains instead of beta chains
- The relaxed form has a low affinity for oxygen
- Adult Hb has a maximum theoretical oxygen-carrying capacity of 1.39 ml O2 per gram of Hb
- Haemoglobin oxygen saturation is a percentage of haemoglobin molecules fully saturated with oxygen
Answers:
- false
- true
- false
- true
- false
Explanation:
- Haemoglobin is an allosteric protein consisting of four globin chains. Each globin is attached to an iron-porphyrin complex (haem moiety).
- Two pairs of globin chains exist within each haemoglobin molecule. Haemoglobin A consists of two α and two β chains (denoted α2β2), while the fetal haemoglobin has α2γ2 configuration.
- It is the principal mode of oxygen transport in the blood.
- Up to four molecules of oxygen can be carried simultaneously by one haemoglobin molecule. This binding of oxygen to Hb is cooperative. When a molecule of oxygen binds to haem, the shape of the globin chain is altered and subsequent oxygen molecules are then bound with greater affinity (relaxed or oxygenated form). This relationship is best described by the sigmoid-shaped oxyhaemoglobin dissociation curve.
- The deoxygenated or taut form has a low affinity for oxygen.
- Haemoglobin has a maximum theoretical oxygen-carrying capacity of 1.39 ml O2 g−1 Hb (known as Hüfner’s constant).
- Haemoglobin oxygen saturation is a percentage expression of the number of oxygen-binding sites occupied out of the maximum number of oxygen binding sites available.
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The ‘EDAIC MCQs with answers and simplified explanations’ section covers a different topic each day with the intent that candidates can prepare one small topic each day, making steady progress in their exam preparation.