haemoglobin oxygen transport
Overview
This lesson explores the structure and function of haemoglobin, the primary protein responsible for oxygen transport in the blood. We will delve into how haemoglobin binds and releases oxygen, the factors influencing this process, and the significance of the oxygen dissociation curve for efficient gas exchange.
Structure of Haemoglobin
Haemoglobin is a **conjugated protein** with a quaternary structure, meaning it is composed of multiple polypeptide chains and a non-protein component. It consists of **four polypeptide chains**, typically two alpha (α) chains and two beta (β) chains in adult haemoglobin (HbA). Each polypeptide chai...
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Key Concepts
- Haemoglobin: A globular protein found in red blood cells, responsible for oxygen transport.
- Heme group: A prosthetic group within haemoglobin containing an iron ion (Fe²⁺) that reversibly binds oxygen.
- Oxyhaemoglobin: Haemoglobin with oxygen bound to its heme groups, giving arterial blood its bright red colour.
- Deoxyhaemoglobin: Haemoglobin without oxygen bound, giving venous blood its darker red/purplish colour.
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Exam Tips
- →Be able to draw and interpret the oxygen dissociation curve, explaining its sigmoidal shape and the significance of the plateau and steep regions.
- →Clearly explain the Bohr effect, detailing how changes in pCO₂ and pH affect haemoglobin's oxygen affinity and the resulting shift in the dissociation curve.
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