Lab 4A Post-lab

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Module 5 Week 1 Assignment: Enzymes. This is a group assignment. You must work with a partner. Please be sure to have joined a group in Canvas and then upload one file for the group. The following kinetic data were obtained for an enzyme in the absence of inhibitor (1) or in the presence of two different inhibitors (2 and 3). The Enzyme concentration was the same in all of the experiments. Graph these data as a Lineweaver-Burke plot. Enzyme mM Inhibitor 2 [S] 1 Inhibitor 3 2 4 8 12 Enzyme (1) 12 20 a. Paste a photo of your Linewaver-Burke plot here. Plot all three lines on one graph. b. Using the date, fill in the following table; 29 35 40 v (umol/ml *sec) Inhibitor (2) 4.3 8 14 21 26 Vmax Km Apparent Vmax Apparent Km Type of inhibition Apparent Vmax Apparent Km Type of inhibition Inhibitor (3) 5.5 9 13 16 18 Click or tap here to enter text. Click or tap here to enter text. Click or tap here to enter text. Click or tap here to enter text. Click or tap here to enter text. Click or tap…

Biochemistry topic question: For the graph shown in the attached image, what is the approximate Vmax______? What is theapproximate Km_____? Please help. Thank you

answer item no. 7-10

Homework 1 (a) The kinetic data given below are for the reaction catalyzed by prostaglandin endoperoxide synthase. Focusing here on the first two columns, determine the Vmax and Km of the enzyme. (b) Ibuprofen is an inhibitor of prostaglandin endoperoxide synthase. By inhibiting the synthesis of prostaglandins, ibuprofen reduces inflammation and pain. Us ing the data in the first and third columns of the table, determine the type of inhibition that ibuprofen exerts on prostaglandin endoperoxi' Rate of formation [Arachidonic acid] (mm) Rate of formation of PGG2 (mm/min) of PGG, with 10 mg/mL ibuprofen (mM/min) 0.5 23.5 16.67 1.0 32.2 25.25 1.5 36.9 30.49 41.8 44.0 2.5 37.04 3.5 38.91

Course : BiochemistryChapter : Amino acid metabolism In the catabolic reaction of amino acids, ammonia is produced as a side compound.Ammonia is so poisonous that it must be removed from the body in the form of urea.Please explaina. the reaction of amino acids with ketoglutarate to produce ammoniab. the urea cyclec. where do reactions a and b occur? Please write the answer on paper ( Handwriting )And provide pict with detail explanation because i want to learn every steps of the processThank you

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Matching Question: Researchers characterized a new enzyme and determined its Km=200 uM. Moreover, they found that at (Etotad10 nM this enzyme reaches maximum reaction velocity Venasa5 is 1. What is the keat of this enzyme? 2. At which concentration of the substrate this enzyme reaches initial reaction velocity (Vo) of 500 nM/s (assuming (Etotal is the same 10 nMy? 3. What is the maximum reaction velocity (Vmax) of the reaction catalyzed by this enzyme at (Etotail4 nM? Make sure to choose the correct units of measure. Note that some of the items from the answer list should NOT be used. v kcat 1. 400 uM - (S] - - Vmax 2 100 uM 500 s 450 uM 250 s1 * 501 7. so00 s 1 UM's SuMis 10 200 uM 11. 10 uMis 12 25 s 13. 500 nM/s

Biochemistry topic question: An enzyme catalyzes a reaction with a with a Km value of 1 × 10–6 M and V max =20mmol/min. At a concentration of 1 × 10–6 M substrate, the rate of the reaction will be: See attached image. Please help. Thank you

Please show all work/answers for the question

Question:- A 10-year old boy recently joined a soccer team and complains of muscle pain and lightheadedness after each of his last three games. Further testing identifies that he has a defect in his lipolysis pathway, specifically a mutation in the lipase that is phosphorylated in response fasting and exercise. (1) Which lipase is defective in this patient? (A) perilipin (B) adipose triglyceride lipase (C) hormone-sensitive lipase (D) monoacylglycerol lipase (E) protein kinase A

ABG RESULT INTERPRETATION PROBABLE CAUSE(S) RT INTERVENTION HCO3 = 17.45 mEq/L BE = -5.12 mmol/L K* = 3.2 mEq/L Na* = 142 mEq/L Ca*+ = 5.2 mEq/L Cl- = 100 mEq/L Glu = 98 mg/dL Lac = 1.5 mEq/L Hь %3D 14.33 g/dL SO2 = 99 % p50 = 23.78 mmHg FiO2 = 40% BİPAP mask

ABG RESULT INTERPRETATION PROBABLE CAUSE(S) RT INTERVENTION HCO3 = 37.12mEq/L BE = 11.11 mmol/L K* = 4.71 mEq/L Na* = 145.9 mEq/L Ca++ = 4.9 mEq/L Cl-= 94 mEq/L Glu = 102 mg/dL Lac = 0.87 mEq/L Hb = 10.56 g/dL SO2 = 90 % p50 = 32.5 mmHg FiO2 = 8 LPM 02 via AEM

Energy calculations They will complete both exercises related to energy calculations. A. Charlie is a 5-year-old, entire, male, mixed breed dog who has been admitted for treatment. The vet has diagnosed pancreatitis. The patient weighs 20 lb and is being fed a wet diet with an energy density of 1460 kcal/kg metabolizable energy (ME). ⚫ Calculate Charlie's Resting Energy Requirement (RER) Calculate how many grams of food this patient needs per day.

Materials - 2021FA-CHM-1O X Bb 4427577 d-fleet02-xythos.content.blackboardcdn.com/6086c260d7e8f/4427577?X-Blackboard-Expiration=1633143600000&X-Blackboard-Sig 6 / 9 100% Exercise 1: Standard Curve for Protein Measurements: A standard curve for protein concentration is often created using known concentrations of bovine serum albumin (protein). This process is called the Bradford Assay; it is a colorimetric assay. A special reagent turns blue when it binds to amino acids present in protein. The intensity of the color is best measured with a spectrophotometer (a device for comparing two light radiations, wavelength by wavelength). In the case of the Bradford Assay the greater the absorbance, the higher the protein concentration. A series of tests were performed on some samples and spectrophotometer: following measurements were obtained using a Protein Concentration (mg/ml) Absorbance (A) 0.26 0.098 0.56 0.213 0.383 0.84 1.12 0.473 1.40 0.527 TASKS: 1. Enter the data into Excel - the…

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Question: Fumerase is an enzyme in the citric acid cycle that catalyzes the conversion of fumerate to L-malate.     Given the fumerate (substrate) concentrations and initial velocities below, construct a Lineweaver-Burk plot and determine Vmax and Km values for the fumerase catalyzed reaction.   Fumerate (mM)                        Rate (mmol l-1 min-1)             2.0                               2.5             3.3                               3.1             5.0                               3.6             10.0                             4.2    Fumerase has a molecular weight of 194,000 and is composed of four identical subunits, each with an active site.     If the enzyme concentration is 1 x 10-8 M for the experiment in part    (a), calculate kcat value for the reaction of fumerase with fumerate.    Note:  units for kcat are reciprocal seconds (s-1).

-YOU MUST ANSWER THE PROBLEMS IN INDEPENDENT ASSESSMENT AND ADDITIONAL ACTIVITIES -PLEASE FOLLOW THE DIRECTION -PLEASE HELP ME OUT THANK YOU SO MUCH IN ADVANCE.

Direction: Answer thoroughly and explain.

C7 Q4:

Please show all work/answers for 1 (d-g)

Please answer and select the best answer in the selection. No need to show the solution as long you answer all question 1 to 8. Thanks for your usual strong support!

Please answer these question. I need these for lab. PRE-LAB ASSIGNMENT – (YOU WILL NOT BE ALLOWED TO BEGIN WORK ON LABWITHOUT THE COMPLETED CALCULATIONS) 1. COMPLETE ALL CALCULATIONS REQUIRED FOR TABLE 1 ( For all measurements, the [PNPP] concentration will be 600 μM in a 1 ml final volume.) PNPP (substrate) stock solution: 100 mM PNPP in buffer 2. IN YOUR LAB NOTEBOOK, DRAW YOUR PREDICTION OF WHAT THEFOLLOWING GRAPHS MIGHT LOOK LIKEa. pH vs. V0b. TEMP vs. V03. OUTLINE THE BEST/MOST EFFICIENT WAY TO PREPARE

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ACTIVITY 9.2.3 Answer the following briefly. 1. What does tocopherol stand for? 2. Differentiate the forms of Vitamin E. 3. Illustrate the relationship between the following: Vitamin E, Vitamin C, Glutathione, alpha-lipoic acid, and Niacin. 4. Why is hemolytic anemia common in premature infants?

Discuss two approaches (methods) based on week-intermolecular forces on detection of ATP over AMP? please explain, hand written answer will be preffered, thanks

P9-11B The following data on baker's yeast in a particular medium at 23.4°C were obtained in the presence and in the absence of an inhibitor, sulfanilamide. The reaction rate (-3) was measured in terms of the oxygen uptake rate Qo, obtained as a function of oxygen partial pressure. (a) Assume the rate Qo, follows Michaelis-Menten kinetics with respect to oxygen. Calcu- late the lo, maximum (i.e., Vmax), and the Michaelis-Menten constant KM- (Ans.: V = 52.63 µL O,/h-mg cells.) (b) Using the Lineweaver-Burk plot, determine the type of inhibition sulfanilamide that causes the O₂ uptake to change. Po, 05 05 35 5.0 Qo, (no sulfanilamide) 00 23.5 33.0 375 42.0 43.0 Qo, (20 mg sulfanilamide/mL added to medium) Page 428 / 993 0.0. 25.6 30.8 36.4 39.6 40.0 Po₂ oxygen partial pressure, mmHg. Qo, = oxygen uptake rate, µL of O₂ per hour per mg of cells. (c) List ways you can work this problem incorrectly. (d) Apply one or more of the six ideas in Preface Table P-4, page xxviii, to this problem. Q+

ABG RESULT INTERPRETATION PROBABLE CAUSE(S) RT INTERVENTION HCO3 = 14.9 mEq/L BE = -10.9 mmol/L K* = 4.6 mEq/L Na* = 140 mEq/L Ca++ = 4.2 mEq/L Cl = 107 mEq/L Glu = 6.5 mg/dL Lac = 11.5 mEq/L Hb = 12.2 g/dL SO2 = 92.4 % p50 = 32.86 mmHg FiO2 = Room Air

EHS 429 MAIN EXAMINATION PAPER 2018 DECEMBER QUESTION TWO (5 Marks each) 2A. Consider the following sets of parallel reactions taking place in the same reactor: A B2C A+B D Reaction (i) Reaction (ii) Kinetics study showed that reaction (i) proceeds at the rate of 0.1 moles per hour (reduction for A and B). On the other hand reaction (ii) proceeds at the rate of 0.2 moles per hour (reduction for A and B and production for D. i. State the overall rate of reaction of the system as a whole. ii. iii. Assuming the reaction rates stay constant how many moles of C and D are produced after 6 hours of reaction? Assuming the reaction rates stay constant how many moles of A and B are removed after 6 hours of reaction? 2B. List the six sequential steps that occur in a typical heterogeneous chemical reaction. 2C. Plot a profile of tracer salt concentration versus time for i) plug low reactor and ii) completely mixed flow reactor assuming that a tracer of known mass is added to the inlet of the…

9:34 AM You sent       Help me with this one Select true if the statement is CORRECT and false if OTHERWISE   1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. 2. Catalysis is defined as the acceleration of a chemical reaction 3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. 4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it 5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity. 6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature. 8. Enzymes can be classified by the kind of chemical…

Practice question #7 chap. 2 p. 145 A. Explain the following observation: cells of E. coli fermenting glucose (anaerobic conditions) grow faster when NO; is supplied to the culture, and then grow even faster when the culture is highly aerated. B. Shiga toxin (Stx) is a potent A-B toxin that inhibits protein synthesis and has a lethal dose 50 (LD50) of approximately 20 ng/kg of body weight in rabbits (meaning that 1 µg of Stx would be lethal for half the people exposed to this dose). Nonetheless, cell lines derived from different mammalian tissues range from highly susceptible (cytotoxic dose 50 [CD50] of approximately 10 pg/ml) to completely resistant (CD50 > 1 µg/ml). What cellular or molecular differences do you think account for susceptibility and resistance of these cell lines? Note: LD50 is the dose at which 50% of the test subjects die. In this case, it was determined for rabbits given intravenous injections of the toxin. CD50 is the concentration at which 50% of the cells die.…

Can I get help with these two questions?