3. Briefly describe and explain the shape of the curve in Q2.
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how to do Q3
![Experiment 1.2 - Reaction over time
2. Using the standard curve in 1.1, calculate the amount of product formed (in M) at each time point in the
following table, then plot a curve of product formation against reaction time.
Absorbance at 415 nm
Cuvette 2+
(PNPP + alkaline
phosphatase)
04
0.404
0.716
1
1
t t
t
له
t
t t
t t
1
t t
1
Time
(min)
90
80
70
60
50
40
30
20
10
0
0
10
ܢ.15
20
25+
30€
35+
40€
50+
60+
70€
80+
90€
0
10
0.936
1.066+
1.1374
1.179
1.203
1.215
1.224
1.228
1.230
1.232
1.234
20
30
40
[PNP] (UM)
Cuvette 2+
(PNPP + alkaline
phosphatase)
0+
24.871
45+
59.194
67.581
72.161
74.871
50
76.419
77.194
77.774
78.032
78.161
78.290€
78.419
PNP
60
70
✔
A
✔
e
e
✔
A
80
90
100
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- a. State TWO (2) advantages of Inductively coupled plasma-optical emission spectroscopy (ICP-OES) over Flame atomic absorption spectroscopy (FAAS).b. What are the TWO (2) advantages of graphite furnace AAS (GFAAS) over flame AAS (FAAS)?c. What is one of the main disadvantages that most flames used in AAShave?Hi :-) Does anyone know how to calculate the amount of an enzyme in mg when you're only given this data: Volume of the original sample containing the enzyme in microlitres. The change in absorbance for the enzyme reaction. The velocity equation. Molar extinction coefficient. Please let me know what formula to use. I'm confused where to begin. Thank you!Result nad Discussion Lead Acetate Reaction: Samples: lysine, cysteine, methionine Reagents: 10% Sodium Hydroxide (NaOH) and Lead Acetate Pb(CH3COO)2 -To 1 ml of the amino acid solution taken in a test tube, add few drops of sodium hydroxide (40%) and boil the contents for 5-10 mins over a bunsen burner. Cool the contents and add few drops of 10% Lead acetate solution and observe.
- SHOW COMPLETE SOLUTION 1. An electrochemical cell consist of 0.2715 Ibs of MnO2, and 0.2524 Ibs of PbO2. A current flow through a 1.1 ohm resistor of electrochemical cell for 45 mins. The reaction takes place at 400k and the total volume of the solution is 504.9 cm^3. Use the standard reduction cell potential table for MnO2 and PbO2: concentration of Mn2+ (2.81 M) and PbO2 (0.95 M) Cell Potential E=0.48 V current when it passes through a 1.1 ohm resistor = 0.44 ampere Determine the following: a. quantity of electricity/charge, Q b. Energy consumed in Joules c. Power in KilowattsIf protein X produces a higher absorbance reading at pH 7 than it does at pH 9, what can you conclude? Question 1 options: A lesser amount of protein X was used in the reaction at pH 7 than at pH 9. A greater amount of protein X was used in the reaction at pH 9 than at pH 7. Protein X is a more efficient catalyst at pH 7 than it is at pH 9. Protein X is a more efficient catalyst at pH 9 than it is at pH 7.For an enzyme kinetics experiment, a student prepared a reaction mixture by mixing 450 microliters of 0.75mM PNPP with 4.25ml of 0.2M Tris-HCl buffer. When he is ready to measure the absorbance, he added 0.3ml of Alkaline Phosphatase to the mixture and mixed thoroughly. What is the substrate concentration at the beginning of the reaction in mM ?
- If an enzyme catalyzed reaction has a KM of 5mM and a Vmax of 60 nm/sec, the substrate concentration at 30 nM/sec is? Thank you.2. The following question tests your lab skills as well as basic knowledge understanding: In Lab1- KHP Determination, 0.85 g moisturized NaOH (M.W.= 40.01 g/mol) solid was dissolved in 500.0 mL of water. 24.21 mL of this NaOH solution was consumed to reach the equivalence point when titrated with 0.2021 g of pure KHP (M.W.=204.22 g/mol. Solid was fully dissolved in 50 mL deionized water). (a). Please write the reaction equation (balanced). Then calculate the precise concentration of NaOH solution. List all steps. (b). What are the primary standard and secondary standard material in the above operation respectively? (c). During the above operation, what glassware/tools were used to measure 0.85 g NaOH, to store 1 liter NaOH solution, to measure pure KHP solid, to conduct the titration, respective ? (d). Can this titration be used to measure the pH value of an unknown solution? Why or why not? (e). Did we use a pH buffer solution in the…Experiment No. 1. Five rabbits were inoculated in the right lung and in the left side of the neck with five minims of sterilized water in which was suspended a sufficient quantity of a pure culture (third generation) of the tubercle bacillus to render the liquid quite perceptibly turbid The needle of the Koch’s inoculating syringe was inserted subcutaneously on the left side of the neck and in the third intercostal space to a depth of thirty millimetres on the right side. These animals were then confined in a small box and put in a dark cellar. They were thus deprived of light, fresh air and exercise and were also stinted in the quantity of food given them while being themselves artificially infected with the tubercle bacillus. Experiment No. 2. Five healthy rabbits were placed under the following conditions: A fresh hole about ten feet deep was dug in the middle of a field, and the animals having been confined in a small box with high sides but no top, were lowered to the bottom of…
- Experiment No. 1. Five rabbits were inoculated in the right lung and in the left side of the neck with five minims of sterilized water in which was suspended a sufficient quantity of a pure culture (third generation) of the tubercle bacillus to render the liquid quite perceptibly turbid The needle of the Koch’s inoculating syringe was inserted subcutaneously on the left side of the neck and in the third intercostal space to a depth of thirty millimetres on the right side. These animals were then confined in a small box and put in a dark cellar. They were thus deprived of light, fresh air and exercise and were also stinted in the quantity of food given them while being themselves artificially infected with the tubercle bacillus. Experiment No. 2. Five healthy rabbits were placed under the following conditions: A fresh hole about ten feet deep was dug in the middle of a field, and the animals having been confined in a small box with high sides but no top, were lowered to the bottom of…Result and Discussion: Pauly Reaction: Samples: tyrosine, alanine, histidine Reagents: Cold Saturated Sulfanilic Acid, Cold 1 % Sodium Nitrite (NaNO2) and 10% Sodium Bicarbonate (Na2CO3) - Mix 0.5 ml of cold saturated sulfanilic acid solution (HANDLE WITH CARE) with 0.25 ml of cold 1.0% NaNO2. Cool in ice with constant shaking for 3 minutes. Add 0.5 ml of the sample and make alkaline with 10% Na2CO3. Record your observation.A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).