3.2 Transport of Oxygen and Carbon Dioxide
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Questions and Answers

What is the main form of transport for oxygen in the blood?

  • Combined with hemoglobin as oxyhemoglobin (correct)
  • Physically dissolved in blood plasma
  • Bound to red blood cells
  • Attached to carbon dioxide molecules
  • Which factor does NOT influence the shape of the oxyhemoglobin dissociation curve?

  • Hemoglobin structure (correct)
  • Temperature
  • Blood pH levels
  • Amount of carbon dioxide in the blood
  • How is most of the carbon dioxide transported in the blood?

  • As carbamino compounds with blood proteins
  • In its gaseous form dissolved in plasma
  • Mainly as bicarbonate ions (correct)
  • Bound to hemoglobin
  • What is described by the term 'hemoglobin saturation'?

    <p>The maximum amount of oxygen that can bind to hemoglobin</p> Signup and view all the answers

    Which physiological effect is associated with the Bohr effect?

    <p>Increased oxygen release in tissues with high CO2 levels</p> Signup and view all the answers

    What is the main role of the protoporphyrin ring in hemoglobin?

    <p>To hold the iron atom for oxygen binding</p> Signup and view all the answers

    Which molecule does oxygen normally combine with when transported in the blood?

    <p>A ferrous atom</p> Signup and view all the answers

    What condition shifts the oxyhemoglobin dissociation curve to the left?

    <p>Carbon monoxide</p> Signup and view all the answers

    When the pH of blood falls, what effect leads to a decrease in the oxygen affinity of hemoglobin?

    <p>Bohr effect</p> Signup and view all the answers

    Which of the following is responsible for promoting oxygen release at the tissue level?

    <p>Lower pH</p> Signup and view all the answers

    What is the effect of most hemoglobinopathies on the oxygen dissociation curve?

    <p>Shift it to the left</p> Signup and view all the answers

    What causes a shift to the right in the CO2 dissociation curve by decreasing its affinity for CO2?

    <p>An increase in oxygen levels</p> Signup and view all the answers

    Which gas binds to hemoglobin with an affinity 210 times greater than oxygen?

    <p>Carbon monoxide</p> Signup and view all the answers

    Which effect is related to CO2 transport in the blood?

    <p>Haldane effect</p> Signup and view all the answers

    What is the function of myoglobin in muscle cells?

    <p>Store oxygen in muscle cells</p> Signup and view all the answers

    What happens to the oxygen dissociation curve in the presence of carbon monoxide?

    <p>Shifts to the left</p> Signup and view all the answers

    What effect does decreased 2,3-diphosphoglycerate (2,3 DPG) have on the oxygen dissociation curve?

    <p>Shift it to the left</p> Signup and view all the answers

    What is the impact of packed cells/banked blood having lower 2,3-DPG levels?

    <p>Shifts the curve to the left</p> Signup and view all the answers

    What is the main determinant of how much oxygen combines with hemoglobin?

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

    What is the normal arterial oxygen content (CaO2) in mL/dL?

    <p>20</p> Signup and view all the answers

    Which equation is used to calculate the oxygen content of the blood?

    <p>(CaO2) = (1.34 x Hb x SaO2) + (PaO2 x 0.003)</p> Signup and view all the answers

    What is the component of the blood's oxygen content that is measured by the PaO2?

    <p>Dissolved oxygen in plasma</p> Signup and view all the answers

    How many molecules/atoms of oxygen can one molecule of Hb combine with?

    <p>4 molecules/8 atoms</p> Signup and view all the answers

    What causes acute intermittent porphyria (AIP)?

    <p>Accumulation of toxic heme precursors</p> Signup and view all the answers

    What is the solubility coefficient of O2 in blood?

    <p>$0.003$ ml O2/100 ml blood/mmHg</p> Signup and view all the answers

    In what state must the iron molecule be to bind oxygen in hemoglobin?

    <p>$Fe^2+$ state</p> Signup and view all the answers

    What factors cause a right shift in the oxygen-hemoglobin dissociation curve?

    <p>Increased PCO2 and decreased pH</p> Signup and view all the answers

    What is the primary effect of the Bohr effect on hemoglobin?

    <p>Facilitates oxygen release</p> Signup and view all the answers

    What causes a left shift in the oxygen-hemoglobin dissociation curve?

    <p>Decreased PCO2 and increased pH</p> Signup and view all the answers

    What is the primary role of 2,3 diphosphoglycerate (2,3 DPG) in the context of hemoglobin?

    <p>Facilitates offloading of oxygen</p> Signup and view all the answers

    In which location does a left shift (reverse Bohr effect) predominantly occur?

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

    Which of the following is responsible for promoting oxygen release at the tissue level?

    <p>Bohr effect</p> Signup and view all the answers

    What is described by the term 'hemoglobin saturation'?

    <p>The percentage of heme groups in hemoglobin that contain bound oxygen</p> Signup and view all the answers

    Which condition shifts the oxyhemoglobin dissociation curve to the left?

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

    The Bohr effect leads to an increase in oxygen affinity of hemoglobin at lower pH levels.

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

    The Haldane effect is primarily associated with oxygen transport in the blood.

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

    An increase in oxygen levels will shift the CO2 dissociation curve to the left, increasing the affinity for CO2.

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

    Carbon monoxide (CO) shifts the oxyhemoglobin dissociation curve to the right.

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

    Hypoventilation causes a right shift in the oxyhemoglobin dissociation curve.

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

    Study Notes

    Transport of Oxygen by the Blood

    • Volume of oxygen delivered to the systemic vascular bed per minute = cardiac output x arterial O2 concentration
    • Content or concentration of O2 (CaO2) is expressed in ml of O2/100 mL of blood
    • Normally expressed as volumes percent = ml O2 per 100 mL of blood
    • Oxygen content (concentration):
      • 3% O2 dissolved in plasma
      • 97% O2 reversibly combined with hemoglobin (Hb)

    Calculating Oxygen Content of the Blood

    • Oxygen content is composed of hemoglobin bound + dissolved
    • Equation for calculating oxygen content of the blood is: (CaO2) = (1.34 x Hb x SaO2) + (PaO2 x 0.003)

    Amount of O2 Dissolved in Plasma

    • Measured by the PaO2 (partial pressure or oxygen tension)
    • Insufficient to fulfill the body's oxygen requirements at rest (normal FiO2 at sea level)
    • Solubility coefficient of O2 = 0.003 ml O2/100 ml blood/mmHg (or per deciliter (dL))
    • Henry's Law: At a temperature of 37°C, 1 mL of plasma contains 0.00003 mL O2/mm Hg PO2

    Oxygen Chemically Combined with Hemoglobin

    • 97% of oxygen delivered to tissues is combined with hemoglobin (Hb)
    • Adult hemoglobin, HbA is a tetramer composed of:
      • 4 heme molecules + 4 globin chains
      • Cells must synthesize all parts except Fe2+
      • Four globin polypeptide chains: 2 α-globin subunits and 2 β-globin subunits
    • A heme molecule is a protoporphyrin ring with a suspended iron molecule
    • Fe in the Fe2+ state binds O2 - Not the Fe3+ state
    • One molecule of Hb combines with 4 molecules/8 atoms of oxygen

    Porphyrins

    • The heme group is a prosthetic group consisting of a protoporphyrin ring and a central, suspended iron atom
    • Acute intermittent porphyria (AIP) is caused by a gene mutation that interferes with cytoplasmic heme synthesis and causes the accumulation of toxic heme precursors
    • Any drug that induces ALA synthase can accelerate this process (barbiturates, etomidate, glucocorticoids, hydralazine)

    Transport of Carbon Dioxide by the Blood

    • Not discussed in this text, but will be covered in the next section

    Bohr and Haldane Effects

    • Right shift = Bohr effect: CO2 and H+ cause Hb to release oxygen
    • Factors that cause a right shift:
      • Increased PCO2 from metabolism
      • Decreased pH - acidosis (ketoacidosis, lactic acidosis, etc)
    • Left shift is due to less [H+] interacting with Hb inside erythrocytes
    • Factors that shift the curve to the left:
      • Decreased CO2
      • Increased pH
      • Decreased Temperature
      • Decreased 2,3 DPG
      • Most hemoglobinopathies

    Myoglobin

    • Myoglobin is a single-polypeptide heme protein that stores O2 in muscle cells
    • Combines with a single molecule O2
    • Structurally similar to a single Hb subunit
    • Hyperbolic dissociation curve
    • P50 far left of HbA
    • O2 remains bound for conditions with lower PO2### Transport of Oxygen by the Blood
    • The volume of oxygen delivered to the systemic vascular bed per minute is calculated by multiplying cardiac output (CO) by arterial O2 concentration.
    • The body has limited stores of oxygen, so limiting cardiac output or pulmonary oxygenation is fatal within minutes.
    • Oxygen content (concentration) is expressed in ml of O2/100 mL of blood and is normally around 20 mL/dL.

    Calculating Oxygen Content of the Blood

    • Oxygen content is composed of hemoglobin-bound and dissolved O2.
    • The equation for calculating oxygen content of the blood is: (CaO2) = (1.34 x Hb x SaO2) + (PaO2 x 0.003).

    Oxygen Delivery to Tissues

    • Oxygen delivery to tissues is approximately 5 mL O2/100 mL blood at rest.
    • Cardiac output is normally 5 L/min, and normal arterial O2 content is 20 mL/dL.
    • Normal venous O2 content is 15 mL/dL.

    Amount of O2 Dissolved in Plasma

    • The amount of O2 dissolved in plasma is measured by the PaO2 (partial pressure or oxygen tension).
    • The solubility coefficient of O2 is 0.003 ml O2/100 mL blood/mmHg.
    • At a temperature of 37°C, 1 mL of plasma contains 0.00003 mL O2/mmHg PO2.

    Oxygen Chemically Combined with Hemoglobin

    • 97% of oxygen delivered to tissues is combined with hemoglobin (Hb).
    • Adult hemoglobin, HbA, is a tetramer composed of 4 heme molecules and 4 globin chains.
    • One molecule of Hb combines with 4 molecules/8 atoms of oxygen.

    Heme Molecule

    • A heme molecule is a protoporphyrin ring with a suspended iron atom (Fe2+).
    • Acute intermittent porphyria (AIP) is caused by a gene mutation that interferes with cytoplasmic heme synthesis.

    Oxygen Transport and Carbon Dioxide

    • Oxygen is transported in the blood as oxyhemoglobin (HbO2) and dissolved O2.
    • Carbon dioxide is transported in the blood as carbamino compounds with blood proteins, bicarbonate, and dissolved CO2.
    • The oxyhemoglobin dissociation curve shows the relationship between the partial pressure of oxygen and the amount of oxygen combined with hemoglobin.

    Porphyrin

    • A porphyrin is a heterocyclic compound containing four pyrrole rings arranged in a square with a metal atom in the central cavity.
    • Porphyrin is a prosthetic group consisting of a protoporphyrin ring and a central, suspended iron atom.

    Cooperative Binding of Hemoglobin (Hb)

    • Hb forms a reversible bond with oxygen, allowing O2 to be released to the tissues.
    • Hemoglobin occurs in two forms: T or "Tense" form (deoxyhemoglobin) and R or "Relaxed" form (oxyhemoglobin).

    O2 Carrying Capacity of Hb

    • The O2 carrying capacity of Hb is the maximal amount of O2 that can bind with Hb.
    • One gram of Hb can combine with 1.34 ml O2.

    Pulse Oximetry

    • Pulse oximetry measures the oxygen saturation of Hb, which is the proportion of oxygenated hemoglobin compared to total hemoglobin.
    • The calculation to find % Hb saturation is: O2 combined with Hb ÷ O2 carrying-capacity of Hb x 100% = % Hb saturation.

    Bohr Effect and Haldane Effect

    • The Bohr effect is the decrease in O2 affinity of Hb when the pH of blood falls, causing Hb to release oxygen.
    • The Haldane effect is the increase in CO2 affinity of Hb when the pH of blood falls, causing CO2 to combine with Hb.
    • The Bohr effect and Haldane effect work in synchrony for uptake and release of O2 and CO2.

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