RBC- Glycolysis
RBC Glycolysis Challenge
Test your knowledge of glycolysis and red blood cell metabolism with this engaging quiz! Delve into the fascinating processes that occur within red blood cells and their essential role in oxygen transport and energy production.
Key Points:
- Understand glycolysis and its importance in red blood cells.
- Explore the Cori cycle and its significance.
- Learn about hemoglobin's cooperative binding to oxygen.
Which of the following is the reason that red blood cells cannot completely oxidize glucose to form carbon dioxide?
They are very small.
They lack mitochondria
They contain a large amount of hemoglobin for oxygen transport.
They lack phosphofructokinase-1 (PFK-1), an essential glycolytic enzyme.
Which statement best describes the Cori cycle?
It regenerates glucose from lactate generated anaerobically in red blood cells and muscle.
It generates fatty acids which can be consumed by red blood cells and muscle.
It regenerates glucose from the products of aerobic respiration generated by red blood cells and muscle.
It generates 2,3 bisphosphoglycerate from 1,3 bisphosphoglycerate for a red blood cellspecific function.
Which molecule, produced by glycolysis in red blood cells, donates electrons to iron to maintain its reduced (Fe2+) state?Pyruvate
Lactate
NADH
ATP
Which molecule produced by glycolysis, or shunts of glycolysis, in red blood cells donates electrons to glutathione to neutralize reactive oxygen species (ROS)?
1,3 bisphosphoglycerate
2,3 bisphosphoglycerate
NADPH
ATP
What are TWO reasons that NADH transfers electrons to iron (via cytochrome b5) in red blood cells?
To neutralize reactive oxygen species (ROS) using electrons transferred from iron
To regenerate NAD+ needed to drive glycolysis forward
To initiate the electron transport chain that is specific to red blood cells
To maintain hemoglobin-bound iron in its reduced (Fe2+) state
To maintain hemoglobin-bound iron in its oxidized (Fe3+) state
Which statement most accurately describes the difference between the T and R states of hemoglobin?
In the R state, hemoglobin has a high affinity for oxygen, while in the T state, hemoglobin has a low affinity for oxygen
In the T state, hemoglobin has a high affinity for oxygen, while in the R state, hemoglobin has a low affinity for oxygen.
In the R state, hemoglobin is bound to oxygen, while in the T state, hemoglobin not bound to oxygen
In the T state, hemoglobin is bound to oxygen, while in the R state, hemoglobin not bound to oxygen.
Examine the graph below, which represents the affinity of hemoglobin and myoglobin at different partial pressures of oxygen. Assume that hemoglobin and myoglobin are both expressed in red blood cells of an animal undergoing intense exercise. Note that this does not happen physiologically! Myoglobin is expressed in muscle cells, and not in red blood cells. The partial pressure of oxygen in the lung is 100 mm Hg, while the partial pressure of oxygen in blood of the veins is 30 mm Hg. Express all of your answers here as a number. Do not include a percentage sign. Approximately what percentage …A…of oxygen is released by myoglobin between the lung and veins? Approximately what percentage of oxygen …..B….is released by hemoglobin between the lung and veins?
A=15
A=60
B=15
B=60
In the image below the affinity of hemoglobin for oxygen is plotted with respect to the partial pressure of oxygen. What statement best describes the physiological basis for the differences between curves A and B?
Curve A represents oxygen binding in the presence of 2,3 BPG, while curve B represents oxygen binding in the veins.
Curve A represents oxygen binding in the lung, while curve B represents oxygen binding in the veins.
Curve A represents oxygen binding in the veins, while curve B represents oxygen binding in the lung.
Curve A represents oxygen binding in the presence of 2,3 BPG, while curve B represents oxygen binding in the lung.
The image below plots the affinity of hemoglobin for oxygen at different partial pressures of oxygen. Three different binding curves are shown, and the solid curve indicates the affinity of hemoglobin at pH 7.4. The curve labeled curve A likely represents hemoglobin binding at (1), and the affinity for oxygen is (2) hemoglobin's affinity for oxygen at pH 7.4. The curve labeled curve B likely represents hemoglobin binding at (3), and the affinity for oxygen is (4) hemoglobin's affinity for oxygen at pH 7.4.
1= a higher pH
1= a lower pH
2= higher than
2=lower than
3=the same pH
3= a lower pH
4=the same as
4=lower than
Lactic acid (1) the affinity of hemoglobin for oxygen. Carbon dioxide (2) the affinity of hemoglobin for oxygen. 2,3 bisphosphoglycerate (3) the affinity of hemoglobin for oxygen
1=increases
1=decreases
2= increases
2=decreases
3=increase
3=decrases
In your own words, describe why hemoglobin's cooperative binding to oxygen is particularly advantageous for exchanging oxygen.
Cooperative binding of oxygen ensures adaptation of the enzymes affinity to the metabolic needs for oxygen binding at low carbon dioxide concentration in the lungs and oxygen release at high carbon dioxide concentration in respiring body tissues. At increasing partial oxygen pressure, saturation of binding sites is increased by the several-fold increase in the affinity of remaining binding sites; whereas, at decreasing partial oxygen pressure in respiring tissues oxygen unloading is promoted by the several-fold lowering of the binding affinity for those sites still occupied by oxygen on the enzyme
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