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OBJECTIVES
At the end of this topic, student should be able to: Describe the basic structure of haemoglobin and its characteristics as respiratory pigments. Explain the transport of carbon dioxide by haemoglobin.
Structure of haemoglobin
Consist of four polypeptide subunits; two chain
two chain held together by hydrogen bond
Structure of haemoglobin
Each peptide contains a haem group, bind with oxygen Therefore, one hemoglobin (Hb) molecule binds up to four oxygen molecules
Hb(O )4
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Combines reversely with O2 to form oxyhaemoglobin in areas of high O2 concentration region - releases O2 in areas of low O2 concentration region
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Air in Lung
As HCO3-,
RBC
Tissue Fluid
Bound to hemoglobin. 2. CO2 is carried 9 to the lungs 1. CO2 diffuses through tissue capillary wall
Only about 7% of the CO2 released by respiring cells is transported/dissolved in blood plasma In plasma,CO2 slowly combine with water to form carbonic acid
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2. As Carbaminohaemoglobin
About 23% CO2 binds to amino ends of the hemoglobin polypeptide chain to form carbaminohemoglobin the amount of CO2 that is able to combine with Hb depends on the amount of O2 already being carried by the Hb
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CONCLUSION
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NEXT LECTURE
17.1 Gaseous exchange and control in mammals c) describe the oxygen dissociation curve of haemoglobin d) compare oxygen dissociation curve of haemoglobin and myoglobin c) explain Bohr effect due to partial pressure of carbon dioxide