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One of the adaptations to high altitude is an increase in the concentration of BPG. What effect does this have on a saturation versus \(p \mathrm{O}_{2}\) curve? Why does increasing [BPG] increase the delivery of \(\mathrm{O}_{2}\) to tissues?

Short Answer

Expert verified
Answer: An increase in BPG concentration at high altitudes decreases hemoglobin's affinity for oxygen, causing a rightward shift in the saturation versus \(pO_2\) curve. This leads to more oxygen being readily released and delivered to tissues despite the lower availability of oxygen in the environment, ensuring the delivery of oxygen to tissues is maintained.

Step by step solution

01

Understand the role of BPG

Bisphosphoglycerate (BPG) is a molecule that binds to hemoglobin, decreasing its affinity for oxygen. This means that when the concentration of BPG increases, hemoglobin is less likely to bind to oxygen. In the context of high altitude adaptations, increased BPG concentrations help the body deliver more oxygen to tissues despite the decreased availability of oxygen in the environment.
02

Analyze the saturation versus \(pO_2\) curve

The saturation versus \(pO_2\) curve shows the percentage of hemoglobin bound to oxygen (saturation) as a function of the partial pressure of oxygen (\(pO_2\)). When BPG concentration increases, the curve shifts to the right. This shift indicates that at any given \(pO_2\), the saturation of hemoglobin with oxygen is lower due to the decreased affinity of hemoglobin for oxygen caused by the increased BPG concentration.
03

Explain the effect of increased BPG concentration on oxygen delivery to tissues

When the saturation versus \(pO_2\) curve shifts to the right due to an increase in BPG concentration, this means that hemoglobin is releasing oxygen more readily. In other words, at any given level of \(pO_2\), more oxygen is available to be delivered to tissues since hemoglobin is bound to less oxygen. This increased release of oxygen allows the body to deliver more oxygen to tissues despite the lower availability of oxygen due to the high altitude.
04

Summarize the impact of high altitude adaptations on BPG concentration and oxygen delivery

In summary, one of the adaptations to high altitude is an increase in BPG concentration, which, in turn, decreases hemoglobin's affinity for oxygen. This leads to a rightward shift in the saturation versus \(pO_2\) curve, allowing for more oxygen to be delivered to tissues despite the lower availability of oxygen in the environment. This adaptation helps the body compensate for the decreased oxygen levels at high altitudes, ensuring the delivery of oxygen to tissues is maintained.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Hemoglobin Oxygen Affinity
Hemoglobin is crucial for transporting oxygen in the blood. Its affinity for oxygen determines how easily hemoglobin picks up oxygen in the lungs and releases it in the tissues. This affinity is influenced by several factors, including pH, temperature, carbon dioxide levels, and the presence of 2,3-bisphosphoglycerate (BPG).

At high altitudes, where oxygen is scarce, the body increases its production of BPG, which binds to hemoglobin and lowers its affinity for oxygen. By doing so, oxygen is more readily released to the tissues where it's needed. This physiological adjustment ensures that vital organs receive sufficient oxygen for their metabolic needs, despite the lower oxygen concentration in the environment.
Saturation vs pO2 Curve
The saturation vs pO2 curve, also known as the oxygen hemoglobin dissociation curve, graphically represents the relationship between the saturation of hemoglobin with oxygen (y-axis) and the partial pressure of oxygen in the blood (x-axis). Normally, this sigmoid-shaped curve signifies how hemoglobin's oxygen binding changes with varying oxygen levels.

When BPG levels rise, the curve shifts to the right, illustrating a decrease in hemoglobin's affinity for oxygen at given pO2 levels. This rightward shift is beneficial at high altitudes, as it allows for more efficient oxygen unloading in the tissues. It ensures that even at lower oxygen pressures, hemoglobin is still able to release sufficient oxygen to meet the metabolic demands of the cells.
High Altitude Adaptations
Adaptation to high altitude involves several physiological changes to optimize oxygen delivery to tissues when there is reduced atmospheric oxygen. In addition to the increase in BPG mentioned earlier, other adaptations include increased breathing rate, increased heart rate, and a long-term increase in the production of red blood cells.

These adaptations improve the body's oxygen transport capacity and facilitate more effective oxygen utilization at the cellular level. High-altitude natives also possess genetic adaptations that enhance their oxygen-carrying capacity, effectively equipping them to thrive in environments where low oxygen levels would otherwise be a significant stressor.
Oxygen Transport in Blood
Oxygen transport in the blood is a finely tuned process centered around hemoglobin, the iron-containing protein in red blood cells. Hemoglobin picks up oxygen in the lungs, where oxygen partial pressure is high, and releases it in the tissues, where the pressure is lower.

Oxygen transport is not only about carrying oxygen to tissues but also ensuring that the oxygen is released where and when it is needed. The body's ability to regulate hemoglobin affinity for oxygen through various effectors, such as BPG, reflects the intricate balance necessary for maintaining efficient oxygen transport under different physiological conditions, including the challenges presented by high altitudes.

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Most popular questions from this chapter

In the three-dimensional structure of immunoglobulins, A. \(\beta\) -sheets align edge to edge. B. in cach chain (H and L) the Cand V regions fold onto one another, forming CV associations. \(\mathrm{C}, \mathrm{C}_{\mathrm{L}}-\mathrm{V}_{\mathrm{L}}\) associations form the complementary sites for binding antigens. D. free-SH groups are preserved to function in forming tight covalent bonds to antigens. E. hinge domains connect globular domains.

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