Haemoglobin and Myoglobin Quiz

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Questions and Answers

What is the difference between haemoglobin and myoglobin in terms of their structure and function?

Haemoglobin consists of four polypeptide chains and possesses four iron-containing haem groups. It is found in RBCs and transports oxygen. Myoglobin consists of one polypeptide chain and possesses one iron-containing haem group. It is found in muscles and stores oxygen.

What is the oxygen-binding capacity of haemoglobin and myoglobin?

Haemoglobin can bind to four oxygen molecules, whereas myoglobin can only bind to one oxygen molecule.

At what partial pressure of oxygen (PO2) do haemoglobin and myoglobin lose oxygen?

Haemoglobin loses oxygen at a PO2 of 60 mmHg, while myoglobin loses oxygen at a PO2 of 20 mmHg.

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Study Notes

Comparison of Haemoglobin and Myoglobin

  • Haemoglobin consists of four polypeptide chains, while myoglobin consists of one polypeptide chain.
  • Each molecule of haemoglobin has four iron-containing haem groups, while myoglobin has one iron-containing haem group.
  • Four oxygen molecules can bind to each molecule of haemoglobin, whereas only one oxygen molecule can bind to each molecule of myoglobin.
  • Haemoglobin is found in red blood cells (RBCs), while myoglobin is found in muscles.
  • Haemoglobin is responsible for transporting oxygen, while myoglobin stores oxygen.
  • Haemoglobin has less affinity with oxygen, meaning it releases oxygen more readily.
  • Haemoglobin loses oxygen at a partial pressure of oxygen (PO2) of 60 mmHg.
  • Myoglobin has more affinity with oxygen, meaning it holds onto oxygen more tightly.
  • Myoglobin loses oxygen at a PO2 of 20 mmHg.
  • Haemoglobin plays a crucial role in oxygen transport throughout the body.
  • Myoglobin is primarily involved in oxygen storage within muscle tissues.
  • The differences in oxygen affinity and oxygen release between haemoglobin and myoglobin contribute to their distinct functions in the body.

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