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Assessment Statements H.6.1 Define partial pressure. H.6.2 Explain the oxygen dissociation curves of adult hemoglobin, fetal hemoglobin and myoglobin.

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Presentation on theme: "Assessment Statements H.6.1 Define partial pressure. H.6.2 Explain the oxygen dissociation curves of adult hemoglobin, fetal hemoglobin and myoglobin."— Presentation transcript:

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2 Assessment Statements H.6.1 Define partial pressure. H.6.2 Explain the oxygen dissociation curves of adult hemoglobin, fetal hemoglobin and myoglobin. H.6.3 Describe how carbon dioxide is carried by the blood, including the action of carbonic anhydrase, the chloride shift and buffering by plasma proteins. H.6.4 Explain the role of the Bohr shift in the supply of oxygen to respiring tissues. H.6.5 Explain how and why ventilation rate varies with exercise. H.6.6 Outline the possible causes of asthma and its effects on the gas exchange system. H.6.7 Explain the problem of gas exchange at high altitudes and the way the body acclimatizes.

3 Define the term partial pressure Atmospheric air is a mixture of gases; nitrogen, oxygen, carbon dioxide, water vapour & inert gases. At sea level, the atmospheric pressure is about kPa. What proportion of atmospheric pressure is due to oxygen?

4 Role of haemoglobin haemoglobin occurs in the red cells haemoglobin molecule is built of four interlocking subunits each subunit is composed of a large globular protein with a non-protein haem group attached, containing iron 1 molecule of oxygen will combine with each haem group, meaning, each haemoglobin molecule is able to transport 4 molecules of oxygen: oxyhaemoglobin is the form in which oxygen is transported from the lungs to the respiring body tissues at respiring tissue cells, oxyhaemoglobin breaks down, releasing oxygen & haemoglobin oxygen is used up by tissue cells while haemoglobin is returned to the lungs to pick up more oxygen

5 the affinity of haemoglobin for oxygen is measured experimentally by finding the percentage saturation with oxygen of blood exposed to air mixtures containing different partial pressures of oxygen the result is called an oxygen dissociation curve oxygen dissociation curve is S-shaped, the amount of oxygen held by haemoglobin depends on the partial pressure of oxygen in the body, too, the amount of oxygen held by haemoglobin depends on the partial pressure in respiring tissues, the oxygen partial pressure is much lower than that in the lungs at lower partial pressures, oxyhaemoglobin breaks down, releasing oxygen in solution and this rapidly diffuses into the surrounding tissues Oxygen dissociation curve

6 Oxygen dissociation curve of adult haemoglobin oxygen dissociation curve for oxyhaemoglobin is S/sigmoid-shaped it shows how the saturation of haemoglobin with oxygen varies with partial pressure of oxygen haemoglobin has an increasing affinity for oxygen, initial uptake of one oxygen molecule by haemoglobin facilitates the further uptake of oxygen molecules low partial pressure of oxygen corresponds to the situation in the tissue, when partial pressure of oxygen is low, oxygen is released low pH, increased carbon dioxide & increased lactic acid causes the curve to shifts the to the right and oxygen is more readily released to respiring tissues – this is known as the Bohr effect high partial pressure of oxygen corresponds to the situation in the lungs, when partial pressure of oxygen is high, oxygen is taken up by haemoglobin Shift to the right; (decreased affinity) low pH, increased CO 2, increased lactic acid

7 Oxygen dissociation curve of fetal haemoglobin between foetal & adult haemoglobin, which one has a higher affinity for oxygen? why it is advantageous that fetal haemoglobin higher affinity for oxygen than adult haemoglobin? like adult haemoglobin, fetal haemoglobin have S-shaped oxygen dissociation curves fetal haemoglobin have a high affinity for oxygen at high partial pressure of oxygen fetal haemoglobin always has a higher affinity for oxygen at corresponding partial pressures of oxygen than adult haemoglobin, thus fetal haemoglobin dissociation curve lies to the left of the adult dissociation curve in the placenta where maternal and fetal blood come into close proximity there is a low oxygen partial pressure fetal haemoglobin must have a greater affinity for oxygen otherwise the maternal oxy-haemoglobin would not dissociate relationship between fetal and adult haemoglobin dissociation curves does NOT change at all partial pressures of oxygen the difference in adult and fetal haemoglobin structures lead to differences in affinity

8 Oxygen dissociation curve of myoglobin myoglobin is a respiratory pigment built of a single haem–globin unit, similar to the four units in haemoglobin myoglobin is only found in skeletal muscle cells, where it acts as a reserve of oxygen myoglobin is specialized for oxygen storage myoglobin has a higher affinity for oxygen than haemoglobin, its dissociation curve is to the left of that for haemoglobin in normal conditions, at rest myoglobin is saturated with oxygen myoglobin is used during intense muscle contraction when the oxygen supply is insufficient i.e. when muscle is very active its oxygen concentration may fall below 0.5 kPa when this happens myoglobin releases oxygen to muscle cells myoglobin oxygen dissociation curve is not sigmoid shaped, it has a steep rise below 5 kPa with no lag & has slower rise approaching 100 % above 5 kPa

9 Oxygen dissociation curves of adult haemoglobin, fetal haemoglobin and myoglobin adult haemoglobin: rapid saturation of oxygen in the lungs rapid dissociation of oxygen as the oxygen concentration decreases oxygen released in the tissues where it is needed fetal haemoglobin: fetal haemoglobin curve to the left of adult haemoglobin higher affinity for oxygen than adult haemoglobin oxygen moves from adult haemoglobin to fetal haemoglobin myoglobin: myoglobin to the left of fetal haemoglobin higher affinity for oxygen than adult haemoglobin only releases oxygen at very low oxygen concentrations in tissues acts as oxygen reserve in muscle cells

10 How carbon dioxide is carried by the blood carbon dioxide is carried in three forms in the blood: carbon dioxide can be dissolved in the blood plasma forming carbonic acid (5 %) carbon dioxide can be carried as dissociated carbonic acid i.e. H + + H CO 3 in red blood cells (85 %) carbon dioxide can be carried as carbaminohemoglobin when it is bound to haemoglobin (10 %) carbonic anhydrase is an enzyme found in red blood cells (erythrocytes) carbonic anhydrase speeds up production of hydrogen carbonate (H CO 3 ) chloride shift i.e. movement of chloride ions into red blood cell, occurs to balance movement of hydrogen carbonate ion out

11 Role of the Bohr shift in the supply of oxygen to respiring tissues hemoglobin carries up to four oxygen molecules Bohr shift promotes the release of oxygen in respiring heart muscle active respiration releases CO 2 causing the partial pressure of CO 2 increases release of CO 2 increases acidity i.e. lowers the pH due to formation of hydrogen ions (H + ) hydrogen ions bind to hemoglobin decreasing hemoglobins affinity for O 2 so O 2 is released from the oxyhemoglobin this occurs due allosteric effect i.e. conformational change in hemoglobin which releases O 2 more readily

12 Bohr shift

13 How and why ventilation rate varies with exercise during exercise the rate of tissue respiration increases i.e. more carbon dioxide produced carbon dioxide production in the tissues exceeds the rate of breathing it out increase in carbonic acid (H 2 CO 3 ), increase in H + ions, pH drops in the blood plasma lactic acid produced during strenuous exercise reduces pH chemoreceptors, located in the carotid & aortic bodies, detect change in pH, increase in carbon dioxide & decrease in oxygen Increased CO2 in the blood & lower pH are also detected by chemoreceptors in medulla nerve impulses sent to the breathing Centre in the medulla of the brain from the chemoreceptors nerve impulses are then sent to diaphragm & intercostal muscles from the breathing Centre in medulla to increase the rate & the depth of breathing ventilation rate is controlled through negative feedback mechanism

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15 Possible causes of asthma and its effects on the gas exchange system asthma is a chronic inflammatory disease of the airway it is caused by allergic reaction to allergens such as; dust, mites droppings, pollen, toxins, pets hairs, fungi etc. immune responses releases histamine which causes: constriction of muscles of wall of bronchioles more mucus is produced these restricts air flow thus ventilation is hard & gas exchange is reduced

16 Problem of gas exchange at high altitudes at high altitudes partial pressure of oxygen is lower, at 7000m P O2 is 8.1 kPa as air is exchanged in lungs hemoglobin does not become fully saturated with O 2 oxygen deprivation of tissues occurs causing fatigue i.e. Monge disease mountain sickness (increased pulse rate, nausea, headaches, sore throat, muscular weakness, dizziness ) may develop ventilation rate & depth increases

17 How the body acclimatizes to high altitudes ventilation rate increases red blood cell (erythrocyte) concentration in blood increases myoglobin concentration in muscles increases capillary networks in the muscles develop greater density lung working volume, vital capacity, increases people living permanently at high altitude develops greater lung surface area

18 Revision Questions Define the term partial pressure. [1] Explain the oxygen dissociation curves of adult haemoglobin, fetal haemoglobin and myoglobin. [6] Describe how carbon dioxide is carried by the blood. [4] Explain, with the use of a diagram, the role of the Bohr shift in the supply of oxygen to respiring heart muscle. [6] Explain the Bohr shift of an oxygen dissociation curve during gas exchange. [6] Explain why ventilation rate varies with exercise. [6] Explain how and why ventilation rate varies with exercise. [6] Outline one possible cause of asthma and its effect on the gas exchange system. [3] Outline how the body acclimatizes to high altitudes. [3] Explain the problem of gas exchange at high altitudes and the way the body acclimatizes. [6]

19 The oxygen dissociation curve is a graph that shows the percentage saturation of haemoglobin at various partial pressures of oxygen. Curve A shows the dissociation at a pH of 7 and curve B shows the dissociation at a different pH. (i) State the possible cause of the curve shifting from A to B. [1] (ii) On the graph, draw the curve for myoglobin. [2]

20 Explain the oxygen dissociation of myoglobin, completing the graph below to support your answer. Po 2 is the partial pressure of oxygen.


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