Explain the usefulness of the Caspase Colorimetric enzyme assays.
Explain the usefulness of the Caspase Colorimetric enzyme assays.
Homework Answers
Answer:
One of the mechanisms of apoptosis is the activation caspases. These enzymes are intracellular cysteine proteases which play a critical role in the execution phase of apoptosis. Apoptosis has been implicated in a number of pathological conditions, including AIDS, cancer and autoimmune diseases
The caspase assays are convenient means of quantitating the enzyme activity of caspases and indirectly quantitate the cell death occurring in different pathological conditions.
Which part of the electromagnetic spectrum is used for colorimetric assays? A. ultraviolet B. infrared C....
Which part of the electromagnetic spectrum is used for colorimetric assays? A. ultraviolet B. infrared C. visible D. ultrasonic
A medical lab technologist is running colorimetric assays for bilirubin levels in newborns and finds that...
A medical lab technologist is running colorimetric assays for bilirubin levels in newborns and finds that one sample falls on the plateau of the calibration curve. What is a good strategy for handling this sample?
Keeping in mind the assays done in Lab 1/2, (a) how could you design a colorimetric...
Keeping in mind the assays done in Lab 1/2, (a) how could you design a colorimetric method to measure alpha-amylase activity? (b) What would you use as a control? (c) At what wavelength should the spectrophotometer be set? (d) Sketch a graph like Plot 1 (from this lab) to represent the amylase activity you would observe using your method. You want to know whether alpha-amylase is more active in the stomach (pH 2) or the intestines (pH 7). (a) How...
1. Research Caspase-2 protease: Indicate i) the class of enzymes to which Caspase-2 belongs, ii) the...
1. Research Caspase-2 protease: Indicate i) the class of enzymes to which Caspase-2 belongs, ii) the kind of bond that is modified by this enzyme, iii) indicate the substrate that is recognised by the enzyme using the amino acid three letter code and iv) whether the enzyme displays high or low substrate specificity.
When running enzyme assays, why do you need to normalize enzyme activity to total protein concentration?...
When running enzyme assays, why do you need to normalize enzyme activity to total protein concentration? What does the specific activity mean in the research lab where enzymes are used? (Hint: are enzymes always pure?)
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. 5 4.5 4 a) What is the KM? KM: v. (mM/s) 3.5 3 2.5 2 1.5 1 0.5 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. a) What is the KM? 5 4.5 4 3.5 3 2.5 2 KM: 3mm V. (mM/s) 1.5 1 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...
You perform a series of enzyme activity assays and then graph the data using a Lineweaver-Burk...
You perform a series of enzyme activity assays and then graph the data using a Lineweaver-Burk plot. You determine the X-intercept is at -0.02 mM-1 and the Y-intercept is at 5.0 (mM/sec)-1. Calculate the Vmax and Km for this enzyme. A. Vmax = 0.20 mM/sec; Km = 50.0 mM B. Vmax = 0.20 mM/sec; Km = ‒50.0 mM C. Vmax = 5.0 mM/sec; Km = 0.02 mM D. Vmax = 5.0 mM/sec; Km = ‒0.02 mM
Explain the usefulness of the concept of “profit” to users of accounting information.
Explain the usefulness of the concept of “profit” to users of accounting information.
#8. Problem 8 on page 63: Explain the usefulness of the coefficient of variation.
#8. Problem 8 on page 63: Explain the usefulness of the coefficient of variation.
Which part of the electromagnetic spectrum is used for colorimetric assays? A. ultraviolet B. infrared C. visible D. ultrasonic
Keeping in mind the assays done in Lab 1/2, (a) how could you design a colorimetric method to measure alpha-amylase activity? (b) What would you use as a control? (c) At what wavelength should the spectrophotometer be set? (d) Sketch a graph like Plot 1 (from this lab) to represent the amylase activity you would observe using your method. You want to know whether alpha-amylase is more active in the stomach (pH 2) or the intestines (pH 7). (a) How...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. 5 4.5 4 a) What is the KM? KM: v. (mM/s) 3.5 3 2.5 2 1.5 1 0.5 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. a) What is the KM? 5 4.5 4 3.5 3 2.5 2 KM: 3mm V. (mM/s) 1.5 1 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...
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