Study Guide for Campbell Biology
11th Edition
ISBN: 9780134443775
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece, Martha R. Taylor, Michael A. Pollock
Publisher: PEARSON
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Chapter 36, Problem 5TYK
Summary Introduction
Introduction: The temperature coefficient is a factor that indicates the rate of change of a reaction as a result when the temperature increases by 10ºC. The temperature coefficient is denoted by Q10. The formula for temperature coefficient is
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It takes 9.4 msec for Enzyme X to catalyse a single reaction when it is fully saturated with substrate. Calculate the Vmax of
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In the graph below, what should the vertical axis be titled?
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6.
8
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16
Time (minutes)
(Accessibility info: One line on graph, uses these coords: 0,0; 2, 025; 4,1; 6,4; 8,7; 10,10; 12,11; 14, 11.25) Curve is slow to rise, up on a
linear slope, slowly flattens at top.)
Lactase (units/ml)
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а.
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С.
Glucose (µM)
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d. Galactose (µM)
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e. Starch (uM)
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O O
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a newly isolated bacterial isocitrate dehydrogenase is found to have a molecular mass of 180 kDa and SDS-PAGE shows it to be a homodimer. 1 mg of enzyme produces a 0.05 moles of product per minute per ml. What is the turnover number of this enzyme in µmole product produced per µmole of enzyme subunit per ml?
a. 4500
b. 4.5
c. 9
d. 9000
Choose the correct answer. Please provide solution with explanation for me to understand. thanks
Chapter 36 Solutions
Study Guide for Campbell Biology
Ch. 36 - Prob. 1IQCh. 36 - a. A flaccid plant cell has a water potential of...Ch. 36 - Prob. 3IQCh. 36 - Prob. 4IQCh. 36 - Prob. 5IQCh. 36 - Prob. 6IQCh. 36 - Prob. 1SYKCh. 36 - Prob. 2SYKCh. 36 - If a plant has a phyllotaxy of alternate leaves...Ch. 36 - Prob. 2TYK
Ch. 36 - Prob. 3TYKCh. 36 - Prob. 4TYKCh. 36 - Prob. 5TYKCh. 36 - Prob. 6TYKCh. 36 - Prob. 7TYKCh. 36 - Prob. 8TYKCh. 36 - Prob. 9TYKCh. 36 - Prob. 10TYKCh. 36 - Prob. 11TYKCh. 36 - Prob. 12TYKCh. 36 - Prob. 13TYKCh. 36 - Prob. 14TYKCh. 36 - Prob. 15TYKCh. 36 - Your favorite houseplant is wilting. Which of the...Ch. 36 - Prob. 17TYKCh. 36 - Which of the following mechanisms explains the...Ch. 36 - Prob. 19TYKCh. 36 - Prob. 20TYK
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- What type of inhibition is observed from the shift of the Lineweaver-Burke plot ahown in the graph below where the solid Ine represents the uninhibited enzymatic reaction while the broken line represents the inhibited enzymatic reaction? A. Irreveraible inhíbítion B. Noncompetitive inhíbition C. Competitive inhíbition D. Uncompetitive inhibition Potassium cyanide ia a polson which combines with cytochrome A3 to prevent binding of oxygen to the enzyme without altering the Km of the reaction with respect to reduced cytochrome c. Which type of inhibition does this represent? A. Irreveraible inhibition c. Competitive inhibition D. Uncompetitive inhibition B. Noncompetitive inhibition _10. Which of the following enzyme classes catalyze reactions in which two molecules become dissociated from each other? A. Kinase в. Нуdrolase c. Isomerase D. Ligase Which of the following enzyme classes catalyze reactions in which two molecules become covalently linked to each other? A. Kinase B. Hydrolase…arrow_forwarda. What is the name of metabolite 1? b. What is the name of metabolite 2? c. What kind of reaction occurred when 1 was converted to 2? d. What general kind of enzyme might you expect to perform this reaction? e. What cofactor, if any, would be required for this reaction?arrow_forwardBased on this graph, it appears that carboxylesterase is most active at a pH of A. 3.5B. 1.5C. 5D. 4arrow_forward
- An amount of 20 uCi of 32p (TR 14.3 d) is injected into the bloodstream of a reference adult ( m =70 kg). 32p is metabolized in such a way that 40% is uniformly distributed throughout the whole body where it is cleared with a biological half-life of 19 d. What is the effective half-life of 32p in the total body? A. 3.26 d B. 14.3 d . C. 8.16 d D. 19 d Clear my choice In the previous problem, calculate the total number of transformations that occur in the total body as a source organ. A. 4.52x1011 B. 3.01x1011 C. 5.22x1011 D. 7.53x1011 In the previous problem, calculate the total body dose (Em=1.710 MeV and E 0.695 Me %3D A. 47.8 mGy B. 47.8 mrad C. 47.8 rad D. 4.78 mradarrow_forwardList the similarities and differences between the followinv coenzymes in terms of structure and fuction. A. Nicotinamide coenzyme B. Flavin coenzyme C. Coenzyme Aarrow_forwardConsider the Michaelis-Menten enzymes below and answer the following questions. Kcat (s') 9.5*105 1.4*10* 2.5*102 1.0*107 5.0*10 8.0*10² Enzyme Km (M) A В a. Which enzyme has the highest affinity substrate? How do you know? b. Which enzyme can convert the most substrate to product in a given period of time? How do you know? c. Which enzyme has the highest catalytic efficiency? How do you know?arrow_forward
- Match each reaction description to the type of enzyme that catalyzes the reaction. 1. Oxidation and reduction of compounds 2. Transfers a functional group from one compound to another compound 3. Utilizes water to break bonds within a compound 4. Addition/removal of a group of atoms and bonds within a compound 5. Forms a bond between two compounds A. Ligase B. Transferase C. Hydrolase D. Oxidoreductase E. Isomerase F. Lyasearrow_forwardAn enzymatic reaction with KM = 4.4 x 10-5 M, is carried out in 400 μL of of solution containing 0.20 nmoles of enzyme. It is observed that Vmax = 6.6 x 10-3 M/s. What is the kcat value for the enzyme? (HINT: Keep an eye on the units)!!! a. 1.50 x 102 s-1 b. 7.56 x 10-5 min-1 c. 1.32 x 104 s-1 d. 3.3 x 106 s-1arrow_forwardUrea is converted to ammonia and carbon dioxide by the action of urease. What will be the effect on the rate if the temperature of the reaction is lowered from 37°C (the optimum temperature) to 27°C? (Circle one). a. There will be no effect. b. The rate will slow down. c. The rate will double. d. The rate will triple.arrow_forward
- Sucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify…arrow_forwardDefine the following terms: a. adenosine triphosphate b. redox reaction c. oxidizing agent d. reducing agent e. NADHarrow_forwarda. What is the name of metabolite 1? b. What is the name of metabolite 2? c. What molecule a is required for this reaction to proceed? d. What molecule b is produced in addition to 2? e. What enzyme performs this reaction?arrow_forward
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