Join thousands of students who trust us to help them ace their exams!Watch the first video
Multiple Choice
Which of the following methods is commonly used to determine enzyme activity levels in a laboratory setting?
A
Determining the amino acid sequence of the enzyme by mass spectrometry
B
Observing changes in enzyme tertiary structure using X-ray crystallography
C
Measuring the rate of product formation over time using a spectrophotometric assay
D
Measuring the enzyme's molecular weight using gel electrophoresis
Verified step by step guidance
1
Step 1: Understand the concept of enzyme activity. Enzyme activity refers to the ability of an enzyme to catalyze a chemical reaction. It is typically measured by monitoring the rate at which a substrate is converted into a product.
Step 2: Recognize the most common method for measuring enzyme activity. Spectrophotometric assays are widely used because they allow researchers to monitor changes in absorbance or fluorescence over time, which correlates with the formation of the product.
Step 3: Learn how spectrophotometric assays work. In these assays, the reaction mixture contains the enzyme, substrate, and any necessary cofactors. As the enzyme catalyzes the reaction, the product either absorbs light at a specific wavelength or fluoresces, and this change is measured using a spectrophotometer.
Step 4: Compare the other methods listed in the problem. Determining the amino acid sequence by mass spectrometry, observing tertiary structure changes using X-ray crystallography, and measuring molecular weight using gel electrophoresis are techniques used for structural or compositional analysis, not for measuring enzyme activity.
Step 5: Conclude that measuring the rate of product formation over time using a spectrophotometric assay is the correct method for determining enzyme activity levels in a laboratory setting.