AQA A-Level Physical Education 7582
The Cardiovascular System
The Respiratory System
The Neuromuscular System
The Musculo-Skeletal System and Movement Analysis
Energy Systems
Skill, Transfer and Practice
Theories of Learning
Guidance and Feedback
Information Processing and Memory
The Emergence and Globalisation of Sport
Equal Opportunities in Sport
Diet and Nutrition
Preparation and Training Methods
Injury Prevention and Rehabilitation
Biomechanical Principles and Levers
Linear and Angular Motion
Projectile Motion and Fluid Mechanics
Personality and Attitudes
Arousal and Anxiety
Aggression
Motivation and Achievement Motivation
Social Facilitation and Group Dynamics
Goal Setting
Attribution Theory
Self-Efficacy and Confidence
Leadership
Stress Management
Concepts of Physical Activity and Sport
Development of Elite Performers
Ethics and Violence in Sport
Drugs in Sport
Sport, the Law and Commercialisation
The Cardiovascular System
Oxygen transport, the Bohr shift and the a-VO₂ difference
- 3 things to know
- Paper 1
Overview
Haemoglobin and myoglobin, the oxyhaemoglobin dissociation curve, the Bohr shift and its causes, the a-VO₂ diff with a worked example, and training adaptations that raise oxygen delivery.
What you need to know
Answer each one before you reveal it.
How is most oxygen carried in the blood?
Where is haemoglobin found, and how much oxygen can one molecule carry?
Questions from this subtopic
Each one with the model answer underneath.
- 1
How is most oxygen carried in the blood?
Model answer
Haemoglobin carries about 97% of oxygen as oxyhaemoglobin. Blood plasma carries the remaining 3% or so in solution.
- 2
Where is haemoglobin found, and how much oxygen can one molecule carry?
Model answer
Haemoglobin is an iron-containing protein in red blood cells. Each haemoglobin molecule can carry four oxygen molecules.
- 3
What is myoglobin?
Model answer
Myoglobin is an iron-containing protein found in muscle fibres, especially slow twitch fibres. Myoglobin stores oxygen and carries it to the mitochondria.
- 4
Why can myoglobin take oxygen from haemoglobin at the muscles?
Model answer
Myoglobin has a higher affinity for oxygen than haemoglobin. Oxygen therefore passes from the blood into the muscle fibre, even at low partial pressures.
- 5
Describe the shape of the oxyhaemoglobin dissociation curve.
Model answer
The curve is S-shaped, or sigmoid. Saturation rises steeply at low partial pressures of oxygen, then levels off near 100% at high partial pressures.
- 6
What does the dissociation curve show about haemoglobin at the lungs?
Model answer
The partial pressure of oxygen in the lungs is high. Haemoglobin becomes almost fully saturated with oxygen at the lungs.
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