Work Sheet 8
1. Describe how the cooperative binding of oxygen by hemoglobin makes it a better oxygen transporter.
2. Define the “R” (relaxed) and “T” (tense) states of hemoglobin.
3. Describe the relationship of the Bohr effect to oxygen binding by hemoglobin and explain the physiological significance of this effect.
4. Discuss the effect of carbon dioxide (CO2) on hemoglobin affinity for oxygen and the physiological relevance of this effect.
5. Explain the effect of 2,3-bisphosphoglycerate (BPG) on hemoglobin affinity for oxygen and how it facilitates oxygen release to tissues.
6. Explain why the low affinity of fetal hemoglobin for BPG is beneficial to the fetus.
Introduction to Antibodies and Antigens
1. Diagram the basic structure common to immunoglobulins.
2. Define the following terms related to immunoglobulin structure: heavy chain, light chain, constant region, variable region, hinge region, Fab fragment, Fc fragment and complementarity-determining regions (CDRs).
3. Describe the different forces involved in the binding of an antibody to its antigen and define the term hapten.
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