Term
| What is the function of Hemoglobin? |
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Definition
Transports O2 to tissue, Transports CO2 away from tissue to the lungs. |
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Term
| What is the function of Myoglobin? |
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Definition
Accepts O2 from Hemoglobin Located in the muscle |
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Term
| What Hemoglobin chains are most present as a fetus? |
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Definition
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Term
What Hemoglobin chains are most present as an adult? |
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Definition
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Term
| What does "Ferrous" mean? and what does it have to do with Hemoglobin? |
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Definition
Ferrous indicates a bivalent iron compound (+2 oxidation state) (as opposed to ferric, which indicates a trivalent iron compound (+3 oxidation state)). If the Fe of Hemoglobin was feric, the oxygen would not bind in a way that would benefit us. |
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Term
| What is the Fe in Heme bound to? |
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Definition
4 pyrrole N-atoms A proximal Histadine An O2 which is also bound to a distal histamine |
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Term
| Why is Oxyhemoglobin red and Deoxyhemoglobin purple? |
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Definition
Color determined by its absorption spectrum.
This spectrum is highly sensitive to degree to which oxygen or other molecules (e.g. CO) is bound to iron |
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Term
| What is the Molecular Extension Coeficiant proportional to? |
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Definition
Light absorption of the molecule. The smaller the number, the more red and less purple. |
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Term
| What is Non-Cooperative binding? |
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Definition
The binding of a ligand(O2 in this case) has nothing to do the the binding of another ligand. This is automatically the case with Myoglobin because it is only one chain. |
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Term
| What is Cooperative binding? |
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Definition
The binding of a ligand(in this case O2) to one binding site influences the binding of a second ligand. This is how Hemoglobin operates. |
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Term
| What is the Keq equation for the binding of Myoglobin? |
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Definition
Keq= [MbO2]/[Mb][O2] products/reactants |
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Term
| How does a high Keq of Myoglobin help us? |
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Definition
It is able to take the O2 from the Hemoglobin. This facilitates the transfer ofoxygen from blood to muscles. |
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Term
| What does P50 stand for on Oxygen Saturation graph? |
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Definition
It stands for the Partial Pressure at which half of the Hemoglobin/Myoglobin will be saturated with O2 |
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Term
| What is the T-state of Hemoglobin? |
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Definition
(tense or taunt) state Deoxyhemoglobin As oxygen binds it increases the likelyhood of more oxygen binding. (cooperative binding) |
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Term
| What is the R-state of Hemoglobin? |
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Definition
relaxed state Oxyhemoglobin |
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Term
| In what form is CO2 transported? |
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Definition
Mostly bicarbonate (HCO3-) 80% Some is carbonmate is bond to Hb |
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Term
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Definition
CO has 220x the affinity for iron than does O2. When CO binds, it puts the Hb in the R-state and causes it to bind tightly to the remaining O2. The bound oxygen is unavailable for tissues. |
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Term
| When would a blood sample be cherry red? |
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Definition
Carboxyhemoglobin (CO poisoning) |
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Term
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Definition
Oxyhemoglobin releases it's O2 when H+ are around (low pH) because Deoxyhemoglobin really wants to bind with H+ Increasing CO2 also has the same effect. Higher pH= more O2 bound to Hemoglobin |
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Term
| 2,3-BPG affect on Hemoglobin |
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Definition
It binds with the T-state of Hemoglobin and kicks off any O2 that may be there. This makes more Oxygen available to tissues. Shifts the oxygen Partial pressure curve to the right. Individuals adapted to a high altitude have more 2,3-BPG binding |
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