Estimating p50 for Hemoglobin/Myoglobin

  • Thread starter Gannon
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In summary, p50 is the partial pressure of oxygen at which hemoglobin or myoglobin is 50% saturated and is an important measure in understanding the oxygen binding capacity of these proteins. It is typically determined experimentally using oxygen saturation spectroscopy and can be influenced by factors such as temperature, pH, and the presence of other molecules. While myoglobin has a higher affinity for oxygen and a lower p50 value, hemoglobin has a lower affinity and a higher p50 value. Estimating p50 has clinical implications for understanding and diagnosing conditions related to oxygen transport, as well as developing treatments and monitoring their effectiveness.
  • #1
Gannon
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http://moodle.lsu.edu/file.php/9836/Homework/HW9.htm"
Part B of the first problem is the one I'm looking at. It asks to "estimate the p50" of each enzyme; how do I do this with what I've been given? Once I have graphed the two, do I find it from the linear equations? Can anyone point me in the right direction?

Thanks.
 
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  • #2
The link doesn't work. Why not just copy the information you were given?
 
  • #3
I have pretty much solved it, though I had a feeling the link wouldn't work. Thanks, though!
 

1. What is p50 and why is it important in relation to Hemoglobin/Myoglobin?

P50 is the partial pressure of oxygen at which hemoglobin or myoglobin is 50% saturated. This means that at this point, half of the available binding sites on the protein are occupied by oxygen molecules. P50 is an important measure in understanding the oxygen binding capacity of these proteins and their ability to transport oxygen to tissues in the body.

2. How is p50 determined for Hemoglobin/Myoglobin?

P50 is typically determined experimentally by measuring the oxygen binding curve of the protein using a technique called oxygen saturation spectroscopy. This involves measuring the absorbance of light at different oxygen concentrations to determine the point at which the protein is 50% saturated with oxygen. P50 can also be calculated using mathematical models based on the protein's structure and oxygen binding properties.

3. What factors affect p50 for Hemoglobin/Myoglobin?

P50 can be influenced by several factors, including temperature, pH, and the presence of other molecules such as carbon dioxide and 2,3-bisphosphoglycerate (BPG). Changes in these factors can alter the shape and stability of the protein, affecting its oxygen binding affinity and thus the p50 value.

4. How does p50 differ between Hemoglobin and Myoglobin?

While both Hemoglobin and Myoglobin are oxygen-binding proteins, they have different structures and functions. Myoglobin has a higher affinity for oxygen than Hemoglobin, meaning it has a lower p50 value and is better able to bind oxygen at lower oxygen concentrations. Hemoglobin, on the other hand, has a lower affinity for oxygen and a higher p50 value, making it better suited for oxygen transport to tissues.

5. What are the clinical implications of estimating p50 for Hemoglobin/Myoglobin?

Estimating p50 can provide valuable information about the oxygen transport capacity of these proteins, which is essential for understanding and diagnosing conditions such as anemia, hypoxia, and carbon monoxide poisoning. It can also help in the development of treatments for these conditions by targeting the factors that affect p50. Furthermore, p50 values can be used to monitor the effectiveness of treatments and track changes in oxygen levels in patients.

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