haemogblobin and dissociation curve

• What is the function of red blood cells?


  To transport oxygen in the blood
• What type of structure does hemoglobin have?

  Quaternary structure
• How many polypeptide chains does hemoglobin contain?

  Four polypeptide chains
• What is the role of heme groups in hemoglobin?

  They contain iron and bind oxygen
• What is myoglobin and how does it differ from hemoglobin?

  Myoglobin stores oxygen at low partial pressures, unlike hemoglobin
• What are the key phrases related to the oxyhemoglobin dissociation curve?

  • Affinity
  • Saturation
  • Loading (Association)
  • Unloading (Dissociation)
• What does the term 'affinity' refer to in the context of hemoglobin?

  It refers to hemoglobin's ability to attract or bind oxygen
• What does saturation mean in relation to hemoglobin?

  Saturation is when hemoglobin holds the maximum amount of oxygen
• What is loading or association in the context of hemoglobin?

  It is when oxygen binds to hemoglobin
• What is unloading or dissociation in relation to hemoglobin?

  It is when oxygen detaches from hemoglobin
• How is the oxyhemoglobin dissociation curve described?

  As a sigmoid curve
• What happens to hemoglobin at high partial pressures of oxygen?


  It becomes almost completely saturated with oxygen
• What is the saturation level of hemoglobin at low partial pressures of oxygen?

  About 50% saturation
• Why is it advantageous for hemoglobin to have a lower affinity for oxygen at low partial pressures?

  It allows hemoglobin to unload oxygen where it is needed
• What is cooperative binding in hemoglobin?

  It is when the binding of one oxygen molecule makes it easier for others to bind
• What is the Bohr effect?

  It describes how high carbon dioxide levels decrease hemoglobin's affinity for oxygen
• What happens to the oxyhemoglobin curve when carbon dioxide levels are high?


  The curve shifts to the right
• What does a rightward shift in the oxyhemoglobin curve indicate?


  It indicates a decrease in hemoglobin's affinity for oxygen
• How does acidity affect hemoglobin's affinity for oxygen?

  Increased acidity decreases hemoglobin's affinity for oxygen
• What is the significance of fetal hemoglobin having a higher affinity for oxygen?


  It allows the fetus to extract oxygen from the mother's blood
• How does llama hemoglobin differ from human hemoglobin?


  Llama hemoglobin has a higher affinity for oxygen at lower partial pressures
• Why do doves have hemoglobin with a lower affinity for oxygen?

  To meet their high metabolic demands during flight
• What advantage does earthworm hemoglobin provide in low oxygen environments?

  It has a higher affinity for oxygen to load it effectively
• What are the key points about hemoglobin and its function?

  • Hemoglobin is a protein with a quaternary structure.
  • It contains four polypeptide chains.
  • Heme groups within hemoglobin bind oxygen.
  • Different types of hemoglobin exist across species.
  • Hemoglobin's affinity for oxygen varies with environmental conditions.
• What are the advantages of different hemoglobin types in various animals?

  • Fetal hemoglobin has a higher affinity for oxygen to extract from maternal blood.
  • Llama hemoglobin is adapted for low oxygen environments.
  • Dove hemoglobin has a lower affinity to meet high metabolic demands.
  • Earthworm hemoglobin can load oxygen effectively in low oxygen conditions.