9. Explain how blood flow to an alveolar area is altered to match airflow to tha
ID: 3523867 • Letter: 9
Question
9. Explain how blood flow to an alveolar area is altered to match airflow to that area. Fig. 17.14 10.Fer each of the follewing explain hew the condition deereases 02 delivery to the -capillaries:-asthma, puln onary edema, emphysema-and-fibrotic1 tung disease. Fig. 18.3- 11. Describe the basic structure of hemoglobin. Which part binds O2? 12. Explain the main features of the Hb-02 saturation curve. Fig. 18.9 Explain the significance of the steep and plateau phases of this curve. 13. Explain the Bohr effect. Fig. 18.9Explanation / Answer
9) The low oxygenated alveoli constricts its surrounding blood vessels,so that the blood should reach to those alveoli where it gets most oxygen.it is believed that the low oxygen concentration causes some undiscovered molecules to be released from alveoli.they diffused to surrounding blood vessels and cause their vasoconstriction.it is suggested that these molecules are released by epithelial alveolar cells when they become hypoxic.
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?The proper partial pressure difference between gases may not be maintained.the carbon dioxide concentration and oxygen concentration becomes equalized by under-ventilation and there is no gas exchange.
?11)Haemoglobin is a 65.5kd protein. It is an oligomeric(constructed from four polypeptide chains,two alpha and two beta chains.each chain is conjugated with heme prosthetic group (tetrapyrole ring).alpha chain contain 141 amino acids and beta chain contain 146 amino acids.
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?the heme prosthetic group is actually a Tetra-pyrole ring linked methylene bridges.The Iron atom present within the center of tetrapyrtole ring coordinated to four nitrogen atoms in the plane,below the plane it is linked to histidine ammino acid and above the plane linked to oxygen molecule.each haemoglobin molecule carries four oxygen atoms attached to four tetrapyrole rings.
13)?The molecular basis behind the Bohr effect is that the deoxyhemoglobin binds hydrogen ion more readily than the oxyhemoglobin.the side chain of histidine beta146 becomes protonated and quaternary structure of deoxyhemoglobin is stablized due formation of ionic interaction.that is why haemoglobin affinity for oxygen at low pH is diminished .
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