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Anna35 [415]
2 years ago
8

Describe 2 ways of salting out proteins ​

Chemistry
1 answer:
liubo4ka [24]2 years ago
8 0

The phenomenon known as "salting-out" occurs at very high ionic strengths, when protein solubility declines as ionic strength rises. As a result, salting out may be used to segregate proteins according to how soluble they are in salt solutions.

Because large levels of sodium chloride disturb the bonds and structure of the active site, the rate of enzyme activity will gradually decrease as the concentration of sodium chloride rises. As a result, some of the active sites get denaturized and the starch loses its ability to attach to them. As more enzymes get denatured and eventually cease to function, enzyme activity will steadily wane.

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Another advantage of advantage of using a microspectrophotometer to analyze fibers asides not causing damage to the sample is that the sample can be quite small.

<h3>What is a microspectrophotometer?</h3>

Microspectrophotometry is a biological technique used to measure the absorption or transmission spectrum of a solid or liquid material in either transmitted or reflected light.

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One advantage of microspectrophotometry is that the sample does not get damaged. However,

However, another advantage of advantage of using a microspectrophotometer to analyze fibers asides not causing damage to the sample is that the sample can be quite small.

Learn more about microspectrophotometry at: brainly.com/question/5832827

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What type of reaction is shown below?
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<span>What type of reaction is shown below? 

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