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- This seems like the correct answer to me but on the input platform it said the asnwer is 7.6x102, is that possible?Three factors were studied: reactor length, carrier flow rate, and sample volume, with the high and low values summarized in the following table. factor high (+1) level low (–1) level X: reactor length 1.3 cm 2.0 cm Y: carrier flow rate 1.6 mL/min 2.2 mL/min Z: sample volume 100 μL 150μL The authors determined the optimum response based on the greatest sensitivity, as determined by the change in potential for the potentiometric detector. The following table summarizes their optimization results. run X* Y* Z* ΔE (mV) 1 –1 –1 –1 37.45 2 +1 –1 –1 31.70 3 –1 +1 –1 32.10 4 +1 +1 –1 27.30 5 –1 –1 +1 39.85 6 +1 –1 +1 32.85 7 –1 +1 +1 35.00 8 +1 +1 +1 32.15 Which factor has the greatest effect on sensitivity (change in potential at the detector)? Which set of conditions optimizes the detection sensitivity?Which statements are TRUE regarding internal standards? I. The response factor is calculated by using a mixture containing known amounts of analyte and internal standard and by using detector response to the analyte and the internal standard. II. Internal standards are useful where instrument response or quantity of sample analyzed varies over time. III. Detector response is inversely proportional to concentration. IV. Detector response to analyte and internal standard is assumed to be constant over a range of concentrations A. I, II, and III B. II, III, and IV C. I and II D. I, II, and IV
- If 5 µM enzyme was used to obtain the data in the summary plot below, V-max = ________________ µM sec-1 and Km = ____________ µM for this enzyme (Enter numeric values to the nearest integer; Do NOT write units.)Hello, can someone please help me? I have already hand graphed 1 and 2 and found the v max, however I cannot find the Km value. I am confused because the plots on the linear weaver burk plot do not extend past the values that make up the line. So how am I supposed to estimate the value for the y-intercept in order to find the Km valueYou are trying to come up with a drug to inhibit the activity of an enzyme thought to have a role in liver disease. In the laboratory the enzyme was shown to have a Km of 1.0 x 10-6 M and Vmax of 0.1 micromoles/min.mg measured at room temperature. You developed an uncompetitive inhibitor. In the presence of 5.0 x 10-5 M inhibitor, the apparent Vmax was determined to be 0.02 micromoles/min.mg. What is the Ki of the inhibitor?
- Sample IdentificationCodeConcentration of M%TA=2-log(%T)Q50004.00 x 10-417.90.75Q50013.20 x 10-425.00.6Q50022.40 x 10-435.70.46Q50031.60 x 10-450.20.3Q50048.000 x 10-570.80.15SampleIdentificationCode%TA=2-log(%T)AMQ0210150143.70.359518560.360.000192Q0210150244.10.355561410.360.00018Q0210150343.80.358525890.360.00017Q0210150444.10.355561410.360.00018Q0210150543.80.358525890.360.00017What was their percent error?43%Does Batch 021015 meet legal requirements?No, because it is not between 2.85 * 10(4) and 3.15 * 10(4)Well #DropsBluedye1234567891012345678910Drops 9Distilled water876543210Concne 0.26tration0.52Test Tube #0.781.041.3Solutions3Concentration (M)2.082.32.6Concentration (ppm)1:1 dilution11.82Starting Dilution21.562:1 dilution0A.Zero standard0Was your calibration curve as linear as you expected?B.Did you experience any âdriftâ of the resistance readings?C.What is the equation of your best-fit line?D.What commercial drink did you analyze?E.Assuming…1. Which of the following is NOT a true representation of the Lineweaver-Burk equation? Group of answer choices a. y-intercept = -1/Vmax b. x-intercept = -1/Km c. y = 1/V0 d. x = 1/[S] e. slope = Km/Vmax 2. If the y-intercept of a Lineweaver-Burk (double reciprocal) plot = 39.37 (sec/millimole) and the slope = 75.3 L/sec, Vmax equals: Group of answer choices a. 75.3 millimoles/sec. b. 0.0254 millimoles/sec. c. 0.523 millimoles/sec. d. 39.4 millimoles/sec. 3. Which of the following is true regarding allosteric enzyme behavior?Group of answer choices a. Allosteric enzymes are rarely important in the regulation of metabolic pathways. b. An allosteric effector binds reversibly on the surface of the enzyme. c. An hyperbolic representation of the relation initial velocity vs [S] is a specific characteristic of an allosteric enzyme behavior. d. Michaelis-Menten kinetics model the kinetic behavior of allosteric enzymes.Chemistry The levels of an organic pollutant (P) in the groundwater at the perimeter of a plant were a cause for concern. A 10 mL sample of the water was taken and the pollutant was extracted with 95% efficiency using 25 mL of diethyl ether. GC was used to analyse the concentration of P in diethyl ether. A calibration curve was plotted for a series of standards of P which yielded the following results: Peak Area Toluene Conc. (µg/ml) 12,000 2.6 23,700 5.0 35,500 7.7 46,800 9.9 31,250 Sample Determine the concentration of P in ppb in the initial groundwater sample.
- calculate the flow rate in ml/hr . order 40meq/l at 10meq/hr in 1000ml in d5w supply 20meq/10ml3) The solution taken from a factory waste sample to prepare an internal standard contains Pb + 2 and Ag + 2, and the analysis peaks were determined as 298 mAU and 324 mAU. To analyze the unknown, a solution containing 0.150 M, 50.0 mL of Ag + 2 is put into the unknown liquid and completed to 100.0 mL. When the peaks are measured again, 670 mAU and 856 mAU signals are read from the samples. What is the concentration of Pb + 2 in the unknown liquid?The Ksp of Zn(OH)2 is 3.00 x 10^-17