Enzyme activity is an important characteristic of enzymes, and its units are moles (M) or milimoles (mM) of substrate produced in a given unit of time (e.g. 1 second). The table below contains data from an analysis of enzyme 1. In this experiment, replicate samples contained the same amount of enzyme, and were supplied with different amounts of substrate. After 10 minutes, the amount of product that had been produced was measured. The equation for enzyme kinetics is shown below to help you think about the reactions at each stage. E+SESE+P 1. Part 1. Graph the activity of enzyme 1, label the X and Y axes, and then answer questions 1-5. (Hint: Identify the dependent variable. Put that on the Y axis) 100 90 80 70 60 50 40 30 20 10 Ō 10 20 30 40 50 60 70 80 90 10⁰ 2. How did enzyme activity respond when the substrate concentration ranged from 0 to 20 mM? 2. Why did enzyme activity respond in this way? 3. How does enzyme activity respond to substrate concentrations from 50 to 100 mM? 4. Why does enzyme activity respond in this way? Enzyme 1 substrate product conc. made in (MM) 10 min. 0 10 20 30 40 50 60 70 80 90 100 0 75 88 90 90.5 89.5 91 89.8 89 90 90

Enzyme activity is an important characteristic of enzymes, and its units are moles (M) or milimoles (mM) of substrate produced in a given unit of time (e.g. 1 second). The table below contains data from an analysis of enzyme 1. In this experiment, replicate samples contained the same amount of enzyme, and were supplied with different amounts of substrate. After 10 minutes, the amount of product that had been produced was measured. The equation for enzyme kinetics is shown below to help you think about the reactions at each stage. E+SESE+P 1. Part 1. Graph the activity of enzyme 1, label the X and Y axes, and then answer questions 1-5. (Hint: Identify the dependent variable. Put that on the Y axis) 100 90 80 70 60 50 40 30 20 10 Ō 10 20 30 40 50 60 70 80 90 10⁰ 2. How did enzyme activity respond when the substrate concentration ranged from 0 to 20 mM? 2. Why did enzyme activity respond in this way? 3. How does enzyme activity respond to substrate concentrations from 50 to 100 mM? 4. Why does enzyme activity respond in this way? Enzyme 1 substrate product conc. made in (MM) 10 min. 0 10 20 30 40 50 60 70 80 90 100 0 75 88 90 90.5 89.5 91 89.8 89 90 90

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 10QP: b. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein...

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What features distinguish enzymes that undergo allosteric control from those that obey Michaelis-Menten equations? Give 2 differences
You design an enzyme assay and choose a substrate concentration equal to the Km of the enzymatic reaction. You measure the rate of the reaction at this substrate concentration to be 75.0 μmol/min. Calculate the Vmax of this reaction in μmol/min. Express your answer with one decimal place. Your previous attempt suffered from low signal-to-noise ratio when you used a substrate concentration equal to the Km. So you decide to increase the substrate concentration to 0.45 mM. You remeasure the rate of the reaction at this new substrate concentration and find it to be 135.0 μmol/min. Using the same Vmax value found above, calculate the Km value of this enzymatic reaction. Express your answer in μM with one decimal place. Considering the previous two questions, what would be the rate of the reaction at a substrate concentration of 0.01 mM? Express your answer in μmol/min with one decimal place.
Is the following true or false? Biocatalysis is limited to the use of enzymes found naturally in yeast or bacteria.
Is the data that you are collecting in the above table quantitative or qualitative? Explain why. Which treatment had the least amount of browning? Which had the most? Why do you think you obtained these results? Remember that the enzyme polyphenol oxidase is a protein! For each treatment, apply your knowledge of how temperature, pH, and salt concentration affect enzyme activity and explain why you got the results that you did. Include bonds and the levels of protein structure that you explored in Activity A in your answer. How does temperature impact the rate of enzyme activity? If you were to leave the apple in the refrigerator longer, why would it eventually brown? Explain based on what you know about enzyme activity. How does pH and its impact on specific types of bonds explain the results you obtained in your lemon juice treatment? Include bonds and levels of protein structure in your answer. How does salt and its impact on specific types of bonds explain the results you obtained…
Is the following statement correct or incorrect? It is only possible to employ enzymes that are present naturally in yeast or bacteria for biocatalysis.
An enzyme with a Km of 3X10-5 M has a lower affinity for its substrate than an enzyme with a Km of 2x10-6 M. Is this true or false?
200 ml of a 2% protein solution containing an enzyme that you want to purify. Half of the sample is subjected to method A, consisting of fractionated precipitations and 5 ml of final solution are obtained, with a concentration protein equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml, with protein richness equal to 10 mg / ml and with an activity enzymatic also equal to 2000 U / ml. You want to know: a) Which of the two methods has provided the purest enzyme. b) By which of the methods the greatest amount of enzyme has been obtained.
200 ml of a 2% protein solution are available, containing an enzyme to be purified. Half of the sample is subjected to method A, consisting of fractionated precipitations, and 5 ml of final solution are obtained, with a protein concentration equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml is obtained, with a protein richness equal to 10 mg / ml, and with an enzymatic activity equal to 2000 U / ml. You want to know: a) Which of the methods has provided the purest enzyme. b) By which of the methods has the greatest amount of protein been obtained.
In the extraction of DNA from Animal cells (for example Blood in Humans), does incubation time with an enzyme reaction solution and proteinase K vary for different sample sources? Why or why not?
Typical activity curves of enzymes that are analyzed in the test tube, like the one presented below, flatten out with time. Provide two possible reasons why this is observed. Must be less than 50 words total
Briefly comment on the differences of using a fixed-time assay versus a kinetic assay to measure enzyme activity. Is it reasonable to assume that the reaction velocity obtained by measuring the amount of product after 30 minutes in a fixed-time assay is directly proportional to absorbance? How could you determine whether this was the case? Word limit 180 words including citation and reference
In the Avery experiment, mice were killed if they injected with S strain cells. Furthermore, incubation with extract from dead S strain cells could transform non pathogenic cells into pathogenic cells. This effect of S strain extract was eliminated if S strain extract is treated with what enzyme before incubation with non-pathogenic cells? protease DNAse RNAse Lipase