The O2-binding curves for normal haemoglobin (Hb A) and a mutant haemoglobin (Hb Kempsey) are shown in the diagram. Which of the following statements, based on this graph, are true?

Human Physiology: From Cells to Systems (MindTap Course List)
9th Edition
ISBN:9781285866932
Author:Lauralee Sherwood
Publisher:Lauralee Sherwood
Chapter11: The Blood
Section: Chapter Questions
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The O2-binding curves for normal haemoglobin (Hb A) and a mutant haemoglobin (Hb Kempsey) are
shown in the diagram. Which of the following statements, based on this graph, are true?
1.0
0.8
Hb/Kempsey
0.6
Hb A
0.4
0.2
0.0
20
40
60
80
100
p02 (torr)
1. Hb Kempsey has a higher affinity for O, than HbA
2. Hb Kempsey is unable to transition between the R and T states
3. Hb Kempsey demonstrates cooperative binding of oxygen.
4. Hb Kempsey's curve could be explained by a loss of nearly all the cooperative interactions
between the subunits.
5. A possible explanation for the curve observed with Hb Kempsey is mutation at His HC3.
2,4,5.
O 1.2,5.
O 1,2,3,4,5.
O 2,3,4.
O 1.2.4.
Y (Fraction Saturation)
Transcribed Image Text:The O2-binding curves for normal haemoglobin (Hb A) and a mutant haemoglobin (Hb Kempsey) are shown in the diagram. Which of the following statements, based on this graph, are true? 1.0 0.8 Hb/Kempsey 0.6 Hb A 0.4 0.2 0.0 20 40 60 80 100 p02 (torr) 1. Hb Kempsey has a higher affinity for O, than HbA 2. Hb Kempsey is unable to transition between the R and T states 3. Hb Kempsey demonstrates cooperative binding of oxygen. 4. Hb Kempsey's curve could be explained by a loss of nearly all the cooperative interactions between the subunits. 5. A possible explanation for the curve observed with Hb Kempsey is mutation at His HC3. 2,4,5. O 1.2,5. O 1,2,3,4,5. O 2,3,4. O 1.2.4. Y (Fraction Saturation)
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