EFFECT OF ENZYMECONCENTRATION ONENZYME ACTIVITYProcedure:1. Prepare 5 test tubes. Place 1 ml of 1%starch and add 10 drops of saliva toeach tube. Mix thoroughly.2. Place the first tube in ice water, the 2ndtube leave at room temperature, the 3rdtube in 400C, the 4thtube at 60oCwater bath and the 5thtube boil for 2minutes..3. Leave the 4 tubes in their respectivetemperatures for 30 minutes. The 4thtubeallows to stand for 30 minutes after heatingfor 2 minutes.4. Test the contents of each tube with iodineand benedict's tests.a. lodine Test – to half of the content of eachtube, add 1 drop of iodine in KIand note the color produced. Compare theintensity of color in each of the6 tubes.b. Benedict's – to 1 ml benedict's reagent,-add 5 drops of the other half ofeach tube and heat in a boiling water bathfor 3 minutes. Note color ofprecipitate 3. What is the effect of temperature below and above the optimum temperature on reactionrate?

Enzymes are the molecules that catalyse the conversion of substrate molecules to products by…

Answered: 3. What is the effect of temperature…

Principles Of Radiographic Imaging: An Art And A Science

6th Edition

ISBN:9781337711067

Author:Richard R. Carlton, Arlene M. Adler, Vesna Balac

Publisher:Richard R. Carlton, Arlene M. Adler, Vesna Balac

Chapter3: Electricity

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1. Why do we need to repeat the measurements of reaction of times ten times?
6. An enzyme catalyzed reaction has a KM of 1 mM and a Vmax of 5 nM/s. What is the reaction velocity when the substrate concentration is (a) 0.25 mM (b) 1.5 mM, and (c) 10 mM?
3. Show that the inverse of equation 29-78 in the textbook gives the Lineweaver-Burk Equation. The hydration of CO2 is catalyzed by the enzyme carbonic anhydrase. For a total enzyme concentration of 2.32 x 10-⁹M, the following data were obtained. [CO2]o (M) v (M/s) 0.00125 2.78 x 10-5 0.00250 5.00 x 10-5 0.00500 8.33 x 10-5 0.02000 1.66 x 10-4 Plot these according to the Burke-Lineweaver Equation and determine the values of Km, the Michaelis constant, and k2, the rate constant for product formation from the enzyme-substrate complex from the slope and intercept of the plotted data.
2. The Km of a particular enzyme is 2.0 x 105 M. If the initial velocity (Vo) is 0.16 mmol/min for [S] = 0.15 M, what will be the initial velocity when [S] =2.0 x 10+M?
2.For question number 1 if a mixture was prepared containing 1 M Glucose 6-Phosphate and 0.001 M Glucose 1-Phosphate the ∆G for this reaction is: included question 1 however, need help with 2 and provided the option for the answer 1.What is the Keq for the conversion of Glucose 1-Phosphate to Glucose 6-Phosphate if the phosphate transfer potential for Glucose 1-Phosphate and Glucose 6-Phosphate are 20.9 kJ/mol and 13.8 kJ/mol respectively?
7. You obtain the following set of data for two enzymes that follow Michaelis-Menten kinetics: Enzyme A Initial velocity (µM/min) 38 Enzyme B Initial velocity (пМ/min) 140 Substrate concentration (µM) 233 350 2 73 4 133 8 229 467 20 400 583 150 706 682 300 750 691 786 798 697 699 1000 3000 6000 800 700 (a) What are the approximate Km values for each enzyme based on these data? Briefly justify your answer. (b) In the above experiment, 0.1 µM of enzyme A or enzyme B were used. Calculate kçat and specificity constant for each enzyme. Which enzyme is more efficient? (c) The kinetics of Enzyme B were re-measured in the presence of a small molecule inhibitor. The Km increased while the Vmax remained unchanged. What type of inhibition is this and why does the Km increase?
1. Calculate the initial velocity (Vo) of a Michaelis-Menten reaction as a fraction of Vmax when [S] = 10Km, when [S] = 0.1Km.
Indicate (in the boxes) the kinetic parameters you can extrapolate from the Lineweaver - Burk Plot. 3. Indicate (in the boxes) the kinetic parameters you can extrapolate from the Lineweaver-Burk Plot. D
2) Below are kinetic data at three different inhibitor concentrations. Graph the data in an appropriate form to determine whether the inhibitor is competitive or uncompetitive. a (μm) 0.4 0.67 1.00 2.00 v (μM/min) (no inhibitor) 0.22 0.29 0.32 0.40 v (μM/min) (10 nM inhibitor) 0.21 0.26 0.30 0.36 v (μM/min) (20 nM inhibitor) 0.20 0.24 0.28 0.32
1. Determine the Michaelis-Menten parameters of Vmax and Kỵ for the reaction S+E E.S E.S+W P+E The rate of reaction is given as a function of substrate: [S] 0.2 0.02 0.01 kmol/m³ -I'S kmol/m³.s E.S k₂E+S 0.54 0.28 0.19 0.005 0.1 0.002 0.045
4. Make a conclusion about the practical reversibility of the reaction at 298K by calculating the constant for the reaction of ATP + AMP 2ADP, AGº=-2.10 kJ / mol.
Experiment #1: The Effect of Concentration on Reaction Rate Number of Drops of Enzyme 2 4 6 Reaction Rate (kPa/min) sgorbyt lov 0.27 0.73 1.29 Experiment #2: The Effect of pH on Reaction Rate pH of Solution 4 7 10 Reaction Rate (kPa/min) 0.36 0.97 0.89 Experiment #3: The Effect of Temperature on Reaction Rate Temperature 10°C 35°C 55°C Reaction Rate 18. Predict what would happen if you added 20 drops of enzyme to the test tube. (kPa/min) 0.58 1.43 0.36 17. What type of relationship exists between substrate concentration and reaction rate? Could you explain why you think this relationship exists?

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