1. PART 2

2. To understand how carbon dioxide influences haemoglobin (The Bohr Effect).

3. The Effect of CO 2 – The Bohr Effect In the presence of an increased concentration of carbon dioxide, the oxygen dissociation curve shifts to the right side of the graph paper!!!!

4. The Effect of CO 2 – The Bohr Effect More Carbon Dioxide combines with water in the blood to form more Carbonic acid. This lowers the pH of the blood (makes it more acidic) and changes the oxygen dissociation curve- the curve shifts to the right. The results: This lowers the haemoglobin’s affinity for it’s oxygen. So more oxygen is released more easily to the respiring tissue. This is called the Bohr effect ppO 2

6. Effect of Carbon dioxide 0 B A partial pressure of oxygen % saturation of Hb CO 2 Partial pressure 3 kPa CO 2 Partial pressure 6kPa ( pH will be lower) 100 80 60 40 20 0

7. Bohr Shift By shifting the curve to the right, oxyhaemoglobin will give up more oxygen at a given partial pressure of oxygen

8. TASK: 1)Write out the flow chart in bold with arrows from the middle of p153 textbook into the space at the bottom of HB p5. 2)Read page 202 of the Heineman book and Do Q 1-3 3)Read page 161 of the AS text book and do Q7

9. By the end of this lesson you should be able to: Describe the habitats of animals that have different types of haemoglobin Describe the oxygen dissociation curves of these animals Explain the advantages of having different types of haemoglobin

10. Lugworm

11. Left shifted curves (fig 4 p154) Partial pressure of O 2 % Saturation of Hb Human Hb Lugworm Hb

14. Can you suggest what conditions animals with this type of haemoglobin may be living in? How has shifting the curve to the left affected the partial pressure at which the Hb is fully saturated? TASK : Use the bottom of textbook p153 and top of p154 to help you to answer the questions in the box on HB p6.

15. HIGHLIGHT THESE SECTIONS AT THE TOP OF HB P6: Animals with haemoglobin with a left shifted curve will be found in habitats where there is very little oxygen (sometimes called anaerobic conditions) Their haemoglobin has an even higher affinity for oxygen than human haemoglobin. This means their haemoglobin takes up more oxygen molecules more readily and can become fully saturated even at very low concentrations of oxygen

16. Foetus

17. Foetal Haemoglobin adult haemoglobin 100 80 60 40 20 partial pressure of oxygen % saturation of Hb foetal haemoglobin

18. Llama

20. Prairie dog

21. Animals which live in extremely low oxygen concentrations of have a curve even further to the left. See p154 NT textbook fig 4, showing the oxygen dissociation curve for the Lugworm (The graph is similar for Blood Worms and Tubifex Worms that live in burrows in mud at the bottom of lakes).

22. Myoglobin An extra Respiratory Pigment just found in the muscle cells of diving mammals only. Myoglobin has an extremely high affinity for oxygen and acts as an oxygen store. The oxygen dissociation curve for myoglobin is a hyperbolic shape.

23. Seal http://www.bbc.co.uk/news/science-environment-26743090

24. Haemoglobin with a right shifted curve has a lower affinity for oxygen. This means that (for a given partial pressure of oxygen) the haemoglobin will give up more oxygen more readily to the respiring muscle cells. This type of haemoglobin is found in very active animals with a high respiration rate eg in shrews, in mackerel fish. RIGHT SHIFTED CURVES HIGHLIGHT THESE SECTIONS AT THE TOP OF HB P7:

25. Haemoglobin of very active animals has a right shifted curve: Mackerel

26. SpeciesPartial pressure of oxygen at which haemoglobin is 50% saturated/kPa Mackerel2.1 Carp0.4

27. MammalBody mass/kgPartial pressure of oxygen at which haemoglobin is 50% saturated/kPa Mouse0.0027.5 Rat0.26.7 Sheep494.8 Human704.3 Horse7253.6 Elephant30003.1

28. MammalBody mass/kgPartial pressure of oxygen at which haemoglobin is 50% saturated/kPa Mouse0.0027.5 Right Shift Rat0.26.7 Right Shift Sheep494.8 Right Shift Human704.3 Horse7253.6 Left Shift Elephant30003.1 Left Shift

30. Myoglobin An extra Respiratory Pigment just found in the muscle cells of diving mammals only. Myoglobin has an extremely high affinity for oxygen and acts as an oxygen store. The oxygen dissociation curve for myoglobin is a hyperbolic shape.

31. Seal

32. TASKS: 1.Do the summary task bottom of HB p7. 2.Circle the correct answer choices on the handout sheet called ‘Comparing Different Types of Respiratory Pigments’. 3.Answer Q1,2,3 from peach box on textbook p155. 4.Do the exam questions Q1,3,4 (sent via e-mail) and bring these with you to next lesson.

33. More Hb TASKS: 1.Read p152-155 AS book carefully. 2.Do the Green box questions Q1-12 on p154-155 and check your own answers with the first column on p250.

34. By the end of this lesson you should be able to: Describe the habitats of animals that have different types of haemoglobin Describe the oxygen dissociation curves of these animals Explain the advantages of having different types of haemoglobin