Carriage of Blood Gases and Haemoglobin Structure
29 Questions
0 Views

Choose a study mode

Play Quiz
Study Flashcards
Spaced Repetition
Chat to lesson

Podcast

Play an AI-generated podcast conversation about this lesson

Questions and Answers

What triggers respiratory compensation for primary metabolic disorders?

  • Change in extracellular pH detected by chemoreceptors (correct)
  • Decrease in minute ventilation due to high PCO2
  • Increased renal bicarbonate reclamation
  • Increase in serum bicarbonate levels
  • How does the body respond to primary metabolic acidosis?

  • Increased renal excretion of bicarbonate
  • Enhanced production of metabolic waste by the liver
  • Decreased minute ventilation
  • Increased minute ventilation and decreased PCO2 (correct)
  • When does renal compensation for primary respiratory disorders typically begin?

  • Within minutes as respiration increases
  • After 6–12 hours of sustained pH changes (correct)
  • Within 24 hours of acidosis onset
  • Immediately upon detection of changed pH levels
  • Which of the following describes the body's response during primary respiratory acidosis?

    <p>Increased excretion of organic acids by the kidneys</p> Signup and view all the answers

    What is the primary factor that affects minute ventilation during metabolic alkalosis?

    <p>Increase in extracellular bicarbonate levels</p> Signup and view all the answers

    What is the primary factor that causes haemoglobin to change from its deoxygenated 'tense' form to its oxygenated 'relaxed' form?

    <p>Binding of oxygen molecules</p> Signup and view all the answers

    At a partial pressure of oxygen of about 40 mmHg, what is the approximate saturation level of haemoglobin?

    <p>77%</p> Signup and view all the answers

    What is the shape of the curve representing the relationship between haemoglobin saturation and oxygen partial pressure?

    <p>Sigmoid</p> Signup and view all the answers

    What happens to the affinity of haemoglobin for oxygen when it is in systemic veins?

    <p>It decreases</p> Signup and view all the answers

    Which molecule plays a crucial role in buffering carbon dioxide in the blood?

    <p>Bicarbonate</p> Signup and view all the answers

    How does oxygen saturation of haemoglobin in the alveoli compare to that in systemic veins?

    <p>Lower in systemic veins</p> Signup and view all the answers

    What physiological condition primarily influences the transition of haemoglobin from its tense to relaxed state?

    <p>Increased partial pressure of oxygen</p> Signup and view all the answers

    What is the role of the haem-iron complex in haemoglobin?

    <p>It facilitates oxygen binding</p> Signup and view all the answers

    What effect does a decrease in blood pH have on the affinity of hemoglobin for oxygen?

    <p>It reduces the affinity for oxygen.</p> Signup and view all the answers

    At which condition does the oxygen dissociation curve shift to the right?

    <p>Increased blood pCO2 levels.</p> Signup and view all the answers

    What is the primary role of 2,3-BPG in human red blood cells?

    <p>To promote the release of remaining oxygen.</p> Signup and view all the answers

    How does increasing temperature affect hemoglobin's affinity for oxygen?

    <p>It reduces the affinity.</p> Signup and view all the answers

    Why is the higher affinity of fetal hemoglobin for oxygen advantageous?

    <p>It allows fetal hemoglobin to extract oxygen from maternal blood.</p> Signup and view all the answers

    What occurs when blood pCO2 levels are low?

    <p>Hemoglobin's affinity for oxygen increases.</p> Signup and view all the answers

    Which of the following statements about 2,3-BPG is TRUE?

    <p>It increases significantly in response to chronic anemia.</p> Signup and view all the answers

    What is the effect of increased hydrogen ion concentration on hemoglobin's oxygen affinity?

    <p>It leads to a rightward shift of the dissociation curve.</p> Signup and view all the answers

    What is the primary role of myoglobin in relation to oxygen?

    <p>It has a greater affinity for oxygen than hemoglobin.</p> Signup and view all the answers

    How is most carbon dioxide transported in the blood?

    <p>In the form of bicarbonate ions.</p> Signup and view all the answers

    Which process is essential for the bicarbonate-ion buffer system to function effectively?

    <p>Carbon dioxide production and hydrogen ion excretion.</p> Signup and view all the answers

    What is the effect of pH changes on hemoglobin's affinity for oxygen?

    <p>Higher pH increases hemoglobin's affinity.</p> Signup and view all the answers

    Which of the following statements about carbonic anhydrase is correct?

    <p>It catalyzes the reaction that converts CO2 and water to carbonic acid.</p> Signup and view all the answers

    What occurs during the chloride shift in red blood cells?

    <p>Bicarbonate ions enter the red blood cells and chloride ions leave.</p> Signup and view all the answers

    In what way do metabolic processes influence bicarbonate concentration?

    <p>By producing carbon dioxide during the Krebs cycle.</p> Signup and view all the answers

    Which of the following organs is involved in hydrogen ion excretion as part of bicarbonate balance?

    <p>Kidney</p> Signup and view all the answers

    Study Notes

    Carriage of Blood Gases

    • Blood carries oxygen and carbon dioxide.
    • Oxygen transport is affected by factors like the oxygen partial pressure, pH, and temperature in different areas of the body.
    • Factors also cause changes in oxygen transport in various parts of the body.
    • Carbon dioxide transport is also important, particularly the bicarbonate buffer system.

    Haemoglobin Structure

    • Haemoglobin is a complex molecule.
    • It's composed of four globin chains (two alpha and two beta).
    • Each globin chain has a haem group, which contains an iron atom that binds oxygen.

    Oxygenated and Deoxygenated Haemoglobin

    • Haemoglobin's structure changes when oxygen binds.
    • In the deoxygenated form, the binding site is narrow, restricting oxygen's access.
    • Binding each oxygen molecule allows the haemoglobin molecule to relax.
    • This easier access allows more subsequent oxygen molecules to bind.

    Hb Saturation with Oxygen and Partial Pressure

    • The relationship between oxygen saturation and partial pressure is sigmoid.
    • In alveoli, the high partial pressure of oxygen leads to almost 100% haemoglobin saturation.
    • Haemoglobin has a high affinity for oxygen in the alveoli.
    • In systemic veins, there's a lower partial pressure of oxygen and a lower Hb saturation (around 77%).
    • This allows oxygen to be released to tissues during aerobic respiration.

    Effect of pH on Haemoglobin Affinity for Oxygen

    • Low pH (high hydrogen ion concentration) reduces haemoglobin's affinity for oxygen.

    • This means that more oxygen is released to tissues in areas of low pH.

    • The curve shifts to the right.

    Effect of PCO₂ on Haemoglobin Affinity for Oxygen

    • High PCO₂ (high carbon dioxide) reduces haemoglobin's affinity for oxygen.

    • This causes more oxygen to be released.

    • The curve shifts to the right.

    Effect of Temperature on Haemoglobin O₂ Affinity

    • Increased temperature reduces the affinity of haemoglobin for oxygen.
    • This causes a rightward shift of the dissociation curve.
    • Decreased temperature increases the affinity of Hb for oxygen and shifts the curve to the left.

    Effect of 2,3-DPG on Haemoglobin Affinity

    • 2,3-BPG is a molecule found in red blood cells.

    • It promotes oxygen release from haemoglobin, particularly in tissues with lower oxygen partial pressures.

    • Levels of 2,3-BPG increase under conditions where oxygen levels are low

    Foetal Haemoglobin Affinity

    • Foetal hemoglobin (HbF) has a higher affinity for oxygen than adult hemoglobin (HbA).
    • This enables efficient oxygen transfer from mother to foetus.

    Myoglobin

    • Myoglobin has a higher oxygen affinity than haemoglobin.
    • Myoglobin stores oxygen in muscle and releases it when the partial pressure of oxygen is low.

    CO₂ Transport in Blood

    • Carbon dioxide is a waste product of metabolism.
    • Most CO₂ is transported as bicarbonate.
    • Carbonic anhydrase catalyses the reaction that converts CO₂ into bicarbonate.
    • Bicarbonate is then transported out of the red blood cell.

    Importance of Bicarbonate Ion

    • The bicarbonate buffering system is crucial for maintaining a stable blood pH.
    • This system can absorb or release hydrogen ions to keep pH constant.
    • It's crucial for regulating many enzyme reactions and the ionization states of various substances, avoiding changes in their structure.
    • Bicarbonate reabsorption in the kidneys maintains pH homeostasis.

    Primary acid-base disorders

    • Changes in ventilation compensate for metabolic disorders.
    • Renal excretion compensates for respiratory disorders.
    • The underlying cause of primary acid-base disorders is evident from the pH, PCO₂, and serum bicarbonate analysis.

    Learning Outcomes

    • Learning objectives focus on understanding respiration, maintaining acid-base balance and respiratory system role in that.

    Studying That Suits You

    Use AI to generate personalized quizzes and flashcards to suit your learning preferences.

    Quiz Team

    Related Documents

    Description

    Explore the fascinating mechanisms of how blood transports oxygen and carbon dioxide. This quiz delves into haemoglobin's complex structure, its binding dynamics, and the factors affecting its oxygen carrying capacity. Test your knowledge on blood gases and learn more about the bicarbonate buffer system.

    More Like This

    Blood Gases and Nutritional Needs
    40 questions
    Blood Gases Lecture 6
    39 questions
    Blood Gases and Respiratory Acidosis
    45 questions
    Use Quizgecko on...
    Browser
    Browser