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Chapter 5: Problem 41

The effect of \(\mathrm{pH}\) on the osmotic pressure of sheep hemoglobin was investigated by Gilbert Adair (Chapter 7). The following data were obtained. $$ \begin{array}{lc} \hline \mathrm{pH} & \text { Osmotic pressure }(\mathrm{mmHg} / \mathrm{I} \text { gprotein } / 100 \mathrm{ml})^{*} \\ \hline 5.0 & 21.5 \\ 5.4 & 13.4 \\ 6.5 & 3.2 \\ 6.7 & 2.4 \\ 6.8 & 2.4 \\ 6.8 & 3.5 \\ 6.8 & 4.5 \\ 7.2 & 5.0 \\ 9.6 & 15.6 \\ 10.2 & 21.4 \\ \hline \end{array} $$ Plot the data and use them to deduce the isoelectric point of sheep hemoglobin.

Short Answer

Expert verified
The isoelectric point of sheep hemoglobin is around pH 6.8, where osmotic pressure is lowest.

Step by step solution

01

Understand the Data

We have a data set with two columns: pH values and corresponding osmotic pressures of sheep hemoglobin in mmHg/g protein/100 ml. We need to use this data to find the isoelectric point.
02

Plot the Data

Create a scatter plot with the pH values on the x-axis and the osmotic pressure on the y-axis. This plot will help us visually assess how osmotic pressure changes with pH.
03

Analyze the Plot for the Isoelectric Point

The isoelectric point is the pH at which a protein carries no net charge and usually corresponds to the minimum osmotic pressure. From the plot, identify the pH value around which the osmotic pressure is at its lowest.
04

Estimate the Isoelectric Point

From the data we plotted, look for the minimum osmotic pressure and identify the nearest pH value. From the plotted data, we notice that 2.4 is the lowest osmotic pressure observed, and it occurs at pH 6.7 and 6.8.

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Key Concepts

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

Osmotic Pressure
Osmotic pressure is a fundamental concept in chemistry and biology, referring to the pressure required to stop the flow of a solvent across a semipermeable membrane. It's driven by differences in solute concentration on either side of the membrane.
When it comes to proteins like sheep hemoglobin, osmotic pressure helps us understand how molecular interactions and environmental conditions impact proteins.
  • Proteins can attract or repel water and solutes, influencing osmotic pressure.
  • In a biological context, osmotic pressure relates to how substances enter and leave cells.
  • High osmotic pressure means water is drawn into an area, which can cause cells to swell or burst, whereas low osmotic pressure means water leaves the area, potentially causing cells to shrink.
Understanding osmotic pressure in relation to proteins is crucial in fields like medicine and biochemistry, where it can affect drug delivery and cell health.
pH Effect on Proteins
The effect of pH on proteins is essential for understanding how proteins behave and function in different environments. pH measures hydrogen ion concentration, determining how acidic or basic a solution is.
Proteins, being composed of amino acids, have unique pH values called isoelectric points, where they carry no net charge.
  • Below the isoelectric point, proteins carry a net positive charge because they gain protons (H+).
  • Above the isoelectric point, they carry a net negative charge as they lose these protons.
  • This charge shift influences protein structure and function, affecting their solubility and interaction with other molecules.
Adjusting the pH changes a protein's charge, which can be used to study its behavior in different conditions, leading to insights into protein stability and function.
Sheep Hemoglobin Analysis
Analyzing sheep hemoglobin involves understanding how its structure and function are influenced by environmental factors like pH. Hemoglobin is a vital protein responsible for oxygen transport in the blood.
In the exercise, different pH levels were tested to observe changes in osmotic pressure, which help determine the isoelectric point of sheep hemoglobin.
  • At the isoelectric point, hemoglobin is least soluble, causing minimum osmotic pressure.
  • Understanding this helps in determining how hemoglobin behaves under physiological conditions.
  • It provides insights into how animals adapt to different pH environments, which can affect oxygen delivery efficiency.
These analyses contribute to a clearer understanding of how hemoglobin functions and can have broader implications in studying other similar proteins across different species.

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Most popular questions from this chapter

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Use the following osmotic pressure data for horse hemoglobin in \(0.2 \mathrm{M}\) phosphate and at \(3{ }^{\circ} \mathrm{C}\) to determine the molecular mass of the protein. $$ \begin{array}{lc} \hline \begin{array}{c} \text { Concentration of } \\ \text { hemoglobin }(\mathrm{g} / \mathrm{I} 00 \mathrm{ml}) \end{array} & \text { Osmotic pressure }\left(\mathrm{cm} \mathrm{H}_{2} \mathrm{O}\right) \\ \hline 0.65 & 3.84 \\ 0.81 & 3.82 \\ 1.11 & 3.51 \\ 1.24 & 3.79 \\ 1.65 & 3.46 \\ 1.78 & 3.82 \\ 2.17 & 3.82 \\ 2.54 & 3.40 \\ 2.98 & 3.76 \\ 3.52 & 3.80 \\ 3.90 & 3.74 \\ 4.89 & 4.00 \\ 6.06 & 3.94 \\ 8.01 & 4.27 \\ 8.89 & 4.36 \\ \hline \end{array} $$
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