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7 Cards in this Set
- Front
- Back
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Structure of Hemoglobin |
Globular protein that consists of 4 polypeptide chains with 4 o2 binding sites. high concentration in RBC Binds O2 in lungs for transport to cells Transport CO2 and H+ from tissues to lungs Carry and release NO into blood vessels |
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Structure of Myoglobin |
single polypeptide chain with one O2 binding site major role is to deliver O2 to the muscles |
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Describe how oxygen binding to hemoglobin is regulated by pH |
As the pH decreases, the affinity of hemoglobin for oxygen decreases, producing the Bohr Effect. |
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Describe how oxygen binding to hemoglobin is regulated by BPG |
Decreases affinity for oxygen BPG binding of Hb stabilizes he T conformation of deoxyhemoglobin. Negatively charged BPG binds to positive residues (not big enough for it to bind in R configuration. Results in release of O2 at higher pO2. |
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Describe isohydric transport of CO2 as bicarbonate. |
CO2 in the lungs is in equilibrium in the blood plasma passing through the lung capillaries. Because the concentration of dissolved CO2 can be adjusted rapidly through changes in the rate of breathing, the bicarbonate buffer system of the blood is in near equilibrium with a large potential reservoir of CO2. |
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Describe the transport of CO2 via carbaminohemoglobin |
binding and NH2 group instead of H2O. |
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Describe the mechanism by which Hb binds and transports NO. |
Go to notes |
