haemoglobin

Cards (57)

  • 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 bind oxygen due to iron content
  • What is myoglobin's function compared to hemoglobin?
    Stores oxygen at low partial pressures
  • 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 hemoglobin's function?
    Ability to attract or bind oxygen
  • What does 'saturation' mean in the context of hemoglobin?
    Maximum amount of oxygen bound to hemoglobin
  • What is 'loading' or 'association' in hemoglobin function?
    Oxygen binding to hemoglobin
  • What does 'unloading' or 'dissociation' refer to?
    Oxygen detaching 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
  • What is the saturation level of hemoglobin at low partial pressures of oxygen?
    About 50% saturation
  • Why is lower affinity for oxygen at low partial pressures advantageous?
    It unloads oxygen where needed
  • What occurs at high partial pressures of oxygen regarding hemoglobin's affinity?
    Hemoglobin has a high affinity for oxygen
  • What is cooperative binding in hemoglobin?
    First oxygen binding eases subsequent bindings
  • What is the Bohr effect?
    Effect of carbon dioxide on hemoglobin's affinity
  • What happens to blood pH when carbon dioxide levels are high?
    Blood becomes more acidic
  • What does a rightward shift in the oxyhemoglobin curve indicate?
    Decreased affinity for oxygen
  • What is the significance of a leftward shift in the oxyhemoglobin curve?
    Increased affinity for oxygen
  • How does fetal hemoglobin differ from adult hemoglobin?
    Fetal hemoglobin has a higher affinity for oxygen
  • Why does fetal hemoglobin need a higher affinity for oxygen?
    To extract oxygen from maternal blood
  • Why do llamas have a leftward shifted hemoglobin curve?
    To adapt to high altitudes with low oxygen
  • What advantage does a rightward shifted curve provide for doves?
    More readily unload oxygen for metabolism
  • How do earthworms adapt to low oxygen environments?
    By having hemoglobin with higher affinity
  • What are the key points about hemoglobin's role in oxygen transport?
    • Hemoglobin is a quaternary protein.
    • It binds oxygen in high partial pressure areas.
    • It unloads oxygen in low partial pressure areas.
    • Cooperative binding enhances oxygen loading.
    • The Bohr effect influences oxygen unloading.
  • How do different types of hemoglobin adapt to their environments?
    • Fetal hemoglobin: Higher affinity for oxygen.
    • Llama hemoglobin: Higher affinity for low oxygen.
    • Dove hemoglobin: Lower affinity for rapid oxygen unloading.
    • Earthworm hemoglobin: Higher affinity for underground oxygen.
  • What is the structure of haemoglobin?
    Quaternary structure with 4 polypeptide chains
  • How many alpha and beta chains does haemoglobin have?
    2 alpha and 2 beta chains
  • What does each haem group in haemoglobin contain?
    A ferrous ion (Fe2+^{2+})
  • How many oxygen atoms can haemoglobin carry?
    Carrying a total of 8 oxygen atoms
  • Why do haemoglobins vary across different organisms?
    Due to differences in extreme environments
  • What happens to haemoglobin in low oxygen environments?
    It allows oxygen to attach easily
  • What is oxyhaemoglobin?
    Haemoglobin combined with oxygen
  • What is the role of haemoglobin in the body?
    Associate with oxygen and dissociate to tissues
  • How does haemoglobin change its affinity for oxygen?
    It changes in certain conditions
  • What occurs when the first oxygen molecule binds to haemoglobin?
    It changes the protein shape for more binding
  • What is positive cooperativity in haemoglobin?
    Binding of one oxygen increases binding of others
  • What does the oxygen dissociation curve illustrate?
    The relationship between oxygen saturation and PO2_{2}
  • What happens at higher partial pressure of oxygen?
    Increases affinity for oxygen in haemoglobin