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Hemoglobin – Blood Cells

by Paul Moss, PhD
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    About the Lecture

    The lecture Hemoglobin – Blood Cells by Paul Moss, PhD is from the course Hematology: Basics.


    Included Quiz Questions

    1. It holds on to oxygen very tightly compared to myoglobin.
    2. It consists of 2 alpha and 2 beta chains.
    3. Iron is a major constituent of haem.
    4. It is not the major form of haemoglobin present at birth
    5. Each globin chain carries a molecule of haem
    1. 4 molecules, 2 alpha chains and 2 beta chains
    2. 4 molecules, 2 alpha chains and 2 gamma chains
    3. 4 molecules, 2 alpha chains and 2 delta chains
    4. 3molecules, 1 alpha chains and 2 beta chains
    5. 3 molecules, 2 alpha chains and 1 beta chains
    1. In the absence of 2,3-BPG, hemoglobin's affinity for oxygen decreases
    2. Myoglobin is a hyperbolic shape in oxygen dissociation curve.
    3. Hemoglobin A has a sigmoid shape in oxygen dissociation curve.
    4. Increase in 2,3 DPG within the red cells can shift the red cell dissociation curve to the right.
    5. When there is a left shift of the oxygen dissociation curve, there is a decrease in the 2,3 DPG.
    1. The protons generated are buffered by the haemoglobin.
    2. Hemoglobin helps in the diffusion of carbon dioxide from tissue to the red cell.
    3. Hemoglobin helps in generation of H2CO3.
    4. Hemoglobin helps in dissociation of H2CO3 into HCO3+ and H+
    5. Hemoglobin is not involved in the transport of CO2

    Author of lecture Hemoglobin – Blood Cells

     Paul Moss, PhD

    Paul Moss, PhD


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