Show calculations for making 10 mls each of the following dilutions of sucrose from the 0.30 M stock solution (Formula #3, Example D) CSTOCK (M) VSTOCK CDESIRED (M) V. DESIRED 0.30 M 0.25 M 0.20 M 0.15 M
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Show calculations for making 10 mls each of the following dilutions of sucrose from the 0.30 M stock
solution (Formula #3, Example D)
CSTOCK (M)
VSTOCK
CDESIRED (M)
V.
X
%3D
X
DESIRED
-- . TI
0.30 M
0.25 M
0.20 M
0.15 М](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fcdccc05c-d411-4be3-87c1-38b5cde54476%2Fd513dd47-33c7-4811-ab60-381c5f535f75%2Flojcyw_processed.png&w=3840&q=75)
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- Substrate Concentration (mol L1) Velocity (mM min-1) 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256 Determine the values of Km and Vmax for the decarboxylation of a 훃-keto acid given the followingdata. You have to plot the graph by using excel and please include the scope of graphYou want to prepare 500 mL of the macronutrient and micronutrient stock solutions which have 100X and 1000X higher concentration, respectively, than the required concentration in the culture mediuma)If 0.17 g/L KH2PO4 is required in MS medium, determine the mass (g) of KH2PO4 that is required to prepare the stock solution and the volume required (mL) to prepare 200 mL MS medium. Show your work.National Board of Medical Examiners Biochemistry Mark 36. In the presence of a metabolite (X), 6-phosphofructokinase is assayed at a fixed concentration of ATP and varying concentrations of fructose 6-phosphate. The resulting data are shown in the table. Fructose 6-phosphate (pM) 5 10 20 40 75 100 200 Velocity umoles/min 0.05 0.15 0.25 0.70 1.7 2.2 3.1 3.1 Velocity (+X) umoles/min 0.006 0.025 0. 10 0.35 1.03 16 2.9 3.1 400 Metabolite (X) is most likely which of the following substances? O A) ADP O B) AMP OC) CAMP D) Citric acid O E) Fructose-2,6-bisphosphate
- after a 5 g onion sample is divided into two equal parts, heat treatment to one of these partsit is being implemented. Then both heat-treated and non-treated parts are 10 times their weightit is ground in an environment containing as much buffer and the determination of pyruvate in the supernatants obtainedit's being done.a) As a result of measurements taken at 520 nm; absorbance value for the heat-treated sample;it was found that the absorbance value in the sample that was not heat treated was 0.123 and the absorbance value in the sample that was not heat treated was 0.520.The equation of the calibration accuracy for pyruvate is that y = 0.1367x – 0.001 (nmol/mL)according to the onion sample; a) independent of alinase activity; b) dependent on alinase activityand c) calculate the total pyruvate amounts in terms of nmol/g of onion.b) How is there a relationship between the activity of the enzyme allinase in onions and the amount of pyruvate?Dec,please explain.(Formulation using Pearson Square Method) Using Pearson Square Method, formulate 50 kilograms of a ration with 18% CP using soybean meal and yellow corn. How much of each ingredient (in kg) should be used in order to satisfy the protein requirement of the animal?The effect of temperature on the hydrolysis of lactose by a ß-galactosidase is shown below in Table 1. The temperature coefficient, Q10 is the factor by which the rate increases by raising the temperature 10°C. The universal gas constant, R is 8.314 J/mol.K. (a) (b) Table 1: Data of Vmax over temperature T (°C) 20 30 35 40 45 Vmax (umoles/min.mg protein) 4.50 8.65 11.80 15.96 21.36 Plot the graph of In Vm vs 1/T using any spreadsheet software (include all appropriate labels and equation). Calculate the activation energy Ea and temperature coefficient Q10.
- Table 1 - Comparison of the effect of catechol concentration on the amount of product formed. Absorbance Potato extract Absorbance 0 mins after 30mins (2nd reading) (mL) 1st reading 1 Tube # la blank 2a 3a 4a 1 1 1 dH₂O Catechol (mL) (mL) 7 5 3 1 0 2 4 6 0.00 0.060 0.033 0-05-2 Q4) Give 2 reasons for adding dH₂O to these tubes in Table 1? Time for reading: 3:21 -0.11 Absorbance: Time for reading: 3.36 Q5) Tube la serves as a control, but why is this control needed? Absorbance: 0.197 Time for reading: 3.37 Based on the data from Table 1 answer these questions: Q1) What is the name of the enzyme found in potato extract? Answer: catechol Q2) What is the substrate? Answer: THO Q3) Name of product of this enzyme catalyzed reaction? Answer: Absorbance: 0.152 Time for reading: 3:39 Absorbance: . 166 ness Catechol Benzoquinone Subtract 1st from 2nd reading -0.01 0-137 0.11.19 0.119 Q6) Notice that your 1st absorbance reading in tubes 2a-4a are quite similar but it then becomes very different…13. 0.9% (m/v) NaCI solution and 5% (m/v) glucose solution are both isotonic to red blood cells. SHOW your work and watch sig figs & units. c. convert the concentration from M to % (m/v) for a 0.342 M NaC solution. (HINT: convert to g/ml and then multiple by 100%)Determine the values of KM and Vmax for the decar-boxylation of a β-keto acid given the following data. You have to plot the graph by using excel. Please include slope Substrate Concentration (mol L1) Velocity (mM min1)2.500 0.5881.000 0.5000.714 0.4170.526 0.3700.250 0.256
- Calculate the concentration of p-aminophenol control to match the 0.075 % w/w limit in 200 mg/10 ml Your Answer: 0.0015% show workCalculcate Kcat for PNP substrate for both enzyme concentrations. enzyme volume: 20 ul Bovine Intensince Alkaline phosphatase molecular weight: 140,000 Bovine intenstine Alkaline phosphatase activity: 300 units/ml and 14 units/mg extinction coefficient PNP: 18.5 abs (mM-1 cm-1) Vmax: 0.332 moles/sec a) enzyme 1 concentration: undiluted b) enzyme 2 concentration: 1:1 dilutionPlease ASAP. Thank you. Explain these results in short answer form. Why was the slope zero for blank solution? What was the optimal concentration for peroxidase activity? Do these values make sense?