Formal lab report (3)

Give two advantages and two disadvantages to using the biuret reaction to measure protein concentration compared to measuring the protein absorbance directly at 280 nm

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Part 1: Assess the following partial results section below by editing it for brevity by omitting any unnecessary parts (1 point), explain why you decided to remove certain sections (1 point): To evaluate inhibitory effects of the selected molecules, 10mM stock solutions of each molecule were prepared in DMSO. A reaction mixture (200μl) was prepared with the same formula optimized for the enzyme activity assay (0.1 M Tris-HCl ph 8, 0.1 M KCI, 25 mM NaCl, 0.25 mM ATP, and two units of inorganic yeast pyrophosphatase) with 10 µM of the sample molecule. The reaction mixture was incubated for 20 minutes at ambient temperature. Enzymatic reaction was triggered by addition of the substrate B (0.2 mM) and the absorbance of the product was monitored at 290 nm for 10 minutes. Six out of 15 sample molecules showed appreciable inhibition at 10 μM (Figure 5). Three of the molecules, A3, A6, and A7 exhibited more than 50% inhibition of the enzyme activity and were further diluted to find the minimal…

Table 4- Determination of the optimum pH of catechol oxidase enzyme Potato extract (mL) Tube # 2d 3d 4d 5d 6d 7d dH₂O (mL) 0 0 0 0 0 0 Catechol (mL) 6 6 6 6 6 6 pH buffer added 4mL pH 2 4mL pH 4 4mL pH 6 4mL pH 7 4mL pH 8 4mL pH 10 1 1 1 1 1 1 Absorbance (0 mins) A: 0.010 Start Time: 3:24 A: 0.008 Start Time: 3:34 A: 0.023 Start Time: 3:36 A: -0.006 Start Time: 3:36 0.018 A: Start Time: 3:36 A: 0.011 Start Time: 3:36 Absorbance (after 10 mins in 40°C water bath) -0.030 A: Take reading at: 3:44 A: 0.154 Take reading at: 3:46 A: 0-105 Take reading at: 3:46 A: 0-132 Take reading at: 3:46 A: 0.074 Take reading at: 3:46 A: 0.018 Take reading at: 3!46 Q15) What is the enzyme's optimum pH(s)? Answer: Q16) Use the difference between 2nd and 1st absorbance to support your conclusion for the optimum pH. Subtract Omin from 10min absorbance -0.04 0.0012 0.082 0.138 0.056 0.007

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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.

In an experiemnt with various temperatures (4°C, 22°C, 50°C and 70°C) to examine how temperature impacts peroxidase activity. State the null hypothesis and alternative hypothesis for this experiment. (Enzyme works best at 50°C)    2. Draw a graph showing relationship of absorbance over time in three cuvettes, (a) one with high amounts of enzyme, (b) one with low amounts of enzyme, and (c) one with medium amounts of enzyme. Assume that the amount of substrate is the same in all three, as is the amount of the dye, guaiacol.  Make sure that you have all the components of the graph including axes titles, units of measurement, legends, etc. 3. A group of researchers varied the concentrations of Fe2+ cofactors added in the solution in which a Hydrogen peroxide + peroxidase reaction took place. They added the cofactor at concentrations = 0.5 ml, 0.4 ml, 0.3 ml, 0.2 ml, 0.1 ml.  A. Draw a graph depicting expected results for this experiment. Make sure that all the components of the graph…

Hi, i dont understand the steps here. Could you rewrite this in a more simple manner so i could understand better. Thanks

Size Size Crude Anion Cation 2) Exclusion Exclusion Lysate Exchange Exchange 1 2 Total Protein Concentration 15.2 6.6 2 3.75 4.7 (mg/mL) Final Sample Volume 60 30 20 4 3 (mL) Enzyme Specific Activity 0.43 1.7 7.25 18.3 12.5 (units/mgprotein) Based on your protein purification sample data, in which of the purification steps in your protocol did you effectively purify your enzyme? Select all that apply. a) anion exchange correct b) cation exchange correct c) size exclusion 1 correct d) size exclusion 2

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ENZYME CATALYSIS LAB EFFECT OF TEMPERATURE   What chemical reaction is being catalyzed in this experiment? Label the substrate(s), enzyme and product(s).

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200 ml of a 2% protein solution containing an enzyme that you want to purify. Half of the sample is subjected to method A, consisting of fractionated precipitations and 5 ml of final solution are obtained, with a concentration protein equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml, with protein richness equal to 10 mg / ml and with an activity enzymatic also equal to 2000 U / ml. You want to know: a) Which of the two methods has provided the purest enzyme. b) By which of the methods the greatest amount of enzyme has been obtained.

True'and false please with brief explanation.

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2.For question number 1 if a mixture was prepared containing 1 M Glucose 6-Phosphate and 0.001 M Glucose 1-Phosphate the ∆G for this reaction is: included question 1 however, need help with 2 and provided the option for the answer 1.What is the Keq for the conversion of Glucose 1-Phosphate to Glucose 6-Phosphate if the phosphate transfer potential for Glucose 1-Phosphate and Glucose 6-Phosphate are 20.9 kJ/mol and 13.8 kJ/mol respectively?

Populate the table with expected results using color codes (-), (+), (++), and (+++). Table 3. Effect of pH on enzyme activity pH of catechol solution Enzyme Activity pH 1   pH 5   pH 7   pH 10   Conclude by defining optimum pH and stating optimum pH value for PPO

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Calculate your dilution strategyto make a 625 ng/mLHRP solution from a 12.5 μg/mL stock given the totalvolume of enzyme youwillneed for your condition this week. Note if you are testing pH, you only need to calculate one enzyme dilution because all other pHs will use the same strategy.

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100 increasing enzyme ativity optimum pH 5 6 9 10 11 7 8 pH 20 40° 60°C Temperature 1. How do pH and temperature affect enzyme activity? 2. What do the graphs suggest about the activity of the enzyme? 3. Draw a graph that represents the role of enzymes in metabolism. (Rubrics on next page.)

Please answer  a and b both

Give two advantages to using the biuret reaction to measure protein concentration compared to measuring the protein absorbance directly at 280 nm.

Dilution factor problem in buffer and unbuffered solution in enzyme.  In factors affecting enzyme activity (pH, temeprature). In testing pH factors, 2% of 4 mL of unbuffered starch solution was added to 4 mL of buffered starch solution, plus the 2mL enzyme solution. However, in testing temperature, 1% of 8 mL buffered starch solution was added to 2mL of enzyme solution. Why use different 1% and 2% starch concentration? My teacher said that in the pH part, upon adding the volumes, it will be diluted to 1%. i don't understand how he got it? If I use M1V1=M2V2, the answer is clearly not 1%.  I am very confused. Thank you.

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Table 2: Effect of pH on Enzyme Activity   pH Absorbance 2 0.05 4 0.35 6 0.8 8 0.5 10 0.4 12 0.1     Use the above data table to complete the following questions: a) Plot the data “pH Vs Abs” using “connect the data point type of graph”. Label the graph with dependent and independent variables where they should be. Provide a title for the graph.   b) Over what pH range does catechol oxidase catalyze catechol to benoquinone?    c) Explain why the graph has a bell-shaped curve.

Using my chart can you help me with the following question. Based on your result, what color do you expect Benedict’s solution to turn in the presence of a simple sugar? Explain what information from your results suggests that Benedict’s solution will turn that particular color when testing a simple sugar?

i. What are the advantages of biological value of protein method compared to N-balance and chemical score? ii. A bull consumes 7 kg DM of feed containing 60 g N/kg. The bull excretes 120 g N in the faeces and 50 g N in the urine. The feacal and urinary N had 20 g metabolic feacal nitrogen (MFN) and 6 g endogenous urinary nitrogen (EUN) respectively. Calculate the BV of the protein in the diet.

Part I. For each of the following four questions: calculate and describe how the requested solution would be made. Please show all of your calculations. In all cases the diluent or solvent will be water. Also, assume the smallest volume you can accurately pipette is 1ul. (CaClh: Molecular weight = 111.0 - NaCl: Molecular weight= 58.44) 1. From a 3M CaCh stock solution, you need to make 600 ml of 9 mM CaClh. Indicate how you would make it. 2. You have a 20ul sample of DNA that you want to run in a gel. You are given 5X track dye; how much track dye do you add to your sample so that the track dye concentration in the sample is 1X? 3. You need to make 6 liters of 20% NaCl solution. Indicate how you wvould make it firom powdered NACI.

7. · In the space provided, sketch a titration curve (pH vs H+ ions dissociated) of a phosphate buffer shown below. The pKa of H2PO4 is 7.0. H,PO, НРО, + 9. 8. 7 pH 3 1.0 0.5 H+ dissociated --> b. What is the effective buffering range of this acid? At what pH will you have 25% of the buffer in the form of H2PO4? с.

please complete the table (volume, dilution factor, concentration of glucose) and determine the concentration of glucose stock solution in mg/mL please show an example of computation

3) Catalase Experiment Food Rate of fizzing (1-10) Boiled potato Raw potato Cooked liver 1 Raw liver 10 Students conducted an experiment to check the rate of enzyme action on different types of food. The table shows the results of an experiment in which students placed hydrogen peroxide on several food samples and recorded the relative amount of fizz that each produced. The fizz was produced by oxygen bubbles released by the action of the enzyme catalase, which is found in almost every living cell. The students conducted a second experiment, using the raw chicken liver from the previous experiment. They modified the chicken liver and used: one whole piece, one piece cut into two, a piece that they pulverized in a blender. ALl the Livers were the same mass. The liver was placed in test tubes and hydrogen peroxide was then added to each. Here are the results: Chicken Liver and Enzyme Action Liver Condition Rate of fizzing whole 9 two pieces 11 pulverized 14 Based on the students'…

Computation: Ratio Strength, PPM, mg%Show your complete solution.1. How many grams of a 1:80 trituration of strychnine sulfate should be used for this prescription?RxStrychnine sulfate 45mgBelladonna extract 360mgSucrose 36gFt. chart; Div. in #XXXVIAmount of Strychnine in grams = ?

An appropriate biochemical buffer should have charges in both its conjugate acid and conjugate base form. This avoids the presence of a neutral form of the buffer that might be able slowly leak into cells. Does unmodified dimethylpiperazine meet this criterion when buffering at pH 8? O Yes No What about buffering at pH 4? D Yes No