What indicates a positive reaction when using the Filter Paper test for oxidase? The presence of what enzyme are we testing for, and what does it say about the species being tested?
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What indicates a positive reaction when using the Filter Paper test for oxidase? The presence of what enzyme are we testing for, and what does it say about the species being tested?
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- Lisa decides to obtain values for the Km and Vmax of an enzyme that was isolated from liver cells.. Using the Michaelis Menten plot. In what kind of measurements are needed and what would be needed to plot on a graph to estimate Km and Vmax?There are six classes of enzymes, namely oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases. (i) (ii) Cell disruption is one of the steps performed during enzyme production. Explain the reason of performing cell disruption in enzyme production and provide THREE (3) enzyme extraction methods for this type of enzyme. Explain the principles of gel electrophoresis as one of the methods used for enzyme purification.Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the followingquestions: (a) How do I run the experiment to find the kinetic properties of the enzyme, KMand Vmax? (b) The enzyme decreased in activity in the presence of NaCl. How do I find out if NaCl is a competitive or non-competitive inhibitor? Explain.
- Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the followingquestions:(a). How do I determine the enzyme activity? Please give the unit. (b) How do I get the specific activity of this enzyme? Please give the unit.Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the followingquestions:During the early stages of an enzyme purification protocol, when cells have been lysed but cytosolic components have not been separated, the reaction velocity-versus-substrate concentration is sigmoidal. As you continue to purify the enzyme, the curve shifts to the right. Explain your results. This is an allosteric enzyme and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly. This is an enzyme that displays Michaelis-Menten kinetics and you purify away an inhibitor. This is an allosteric enzyme and during purification you purify away an activator. This is an allosteric enzyme displaying a double-displacement mechanism and during purification you purify away one of the substrates: This is an enzyme that displays Michaelis-Menten kinetics, and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly.
- Table 2: Effect of pH on Enzyme Activity pH Absorbance 2 0.05 4 0.35 6 0.8 8 0.5 10 0.4 12 0.1 Use the above data table to complete the following questions: a) Plot the data “pH Vs Abs” using “connect the data point type of graph”. Label the graph with dependent and independent variables where they should be. Provide a title for the graph. b) Over what pH range does catechol oxidase catalyze catechol to benoquinone? c) Explain why the graph has a bell-shaped curve.Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the following questions:(a) How do I determine the protein/enzyme concentration? Please give the unit.(nmol/min) 30 31 32 33 34 35 A student performed a lactate dehydrogenase (LDH) assay multiple times with varying amounts of substrate added to the reaction mixture. All other conditions were kept the same. This graph shows the results observed: 100 75 10 20 30 40 Lactate concentration (nmol/ml) Why is this student not detecting a linear increase in reaction rate at higher substrate concentrations? T TTArial v 3 (12pt) * T.=,三, 日iu 4:03 PM to search 5/6/2021
- Following is the Michaelis-Menton graphs of 2 substrates for the same enzyme. What are the correct value of I and II for the two substrates A and B? A : I= 0.25 , II= -3.3 B: I= 0.2 , II= -0.25 A: I= 0.125 , II= -0.67 B: I= 0.17 , II= -2.0 A : I= 0.17 , II= 2 B: I= 1.5 , II= 0.67 A : I= 0.25 , II= -1.5 B: I= 0.2 , II= -0.5You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphataseTwo different preparations of the same enzyme are characterized below. Total protein (mg) Total activity (activity units) Step Volume Specific activity (ml) Preparation 1 300 1000 600,000 Preparation 2 200 1000 500,000 a) Fill in the 3 double-underlined blanks on the table below. b) Which of the 2 preparations would you think is likely to be more pure? Explain.