After doing the preliminary studies on redcrest protein extract, Tighnari proceeded with its characterization and analysis proper. He purified the crude protein extract through ammonium sulfate precipitation (40-60%) and gel filtration chromatography. Shown below are the results of the analyses.
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- How would you make two-fold serial dilutions such that the last tube is a 1:32 dilution of the original, concentrated material? Assume that you need to have at least 500 µl of each dilution, and you should be able to perform the dilutions in microfuge tubes with a maximum capacity of 1.5 ml.In performing the Kirby-Bauer procedure in a clinical laboratory setting, why must the agar be a certain depth? Why must the absorbance of the inoculum be standardized?Using 25 μL of serum, how much diluent would be needed to create a 1:2 dilution? ______ μL
- Determine the concentration of L. monocytogenes enumerated from the apple slice based on the information below. You must draw your serial dilution and show your mathematical calculation. The apple slice (12 g) was first mixed with 108 ml of sterile 0.1% peptone water. After, 1 ml was added to tube containing 9 ml of sterile 0.1% peptone water. Process was repeated with two additional tubes. 1 ml was pipetted from tubes 2 and 3 onto MOX media. Plates were incubated at 37 for 48 hours. The pictures below show the plates from tube 2 (left) and tube 3 (right).You will be given 1 mL of a 2.0 mg/mL solution of bovine serum albumin (BSA) and 1 mL of a 2.0 mg/mL solution of bovine gamma globulin (BGG). From these solutions, you will need to make 100 μL of each of the following standards using 1x MBP purification buffer as the diluent for preparation of a standard curve: 1000 μg/mL, 750 μg/mL, 500 μg/mL, 250 μg/mL, 125 μg/mL, and 0 μg/mL.Explain how gel filtration chromatography works. What type of gel will you used when the protein size is 2500 Da? Explain.
- 4 mL of 10% TCA solution was added to 1 mL of serum and after mixing, it was waited for two minutes and filtered through non-phosphorus filter paper. 1 mL of the filtrate was taken and 13 mL of distilled water, 4 mL of sulfomolybdic acid and 2 mL of dilute SnCl2 solution were added and mixed, and after waiting for 15 minutes, the absorbances of the obtained solutions against pure water at 520 nm were read. If the function of the calibration graph obtained with 0.5-2.5 mg/mL standard phosphorus solutions is y= 0.245x + 0.107 and the absorbance value of the serum sample is 0.109, what is the amount of phosphorus in the sample?Gel-filtration chromatography is a useful method for removing salts, such as ammonium sulfate, from protein solutions. Describe how such a separation is accomplished.In Gel filtration chromatography, when will you stop collecting eluents if sample is not colored?
- Following electrophoresis of the two pGlo mini-preparation samples (both digested and undigested), the following agarose gel image was obtained. provide an accurate and detailed figure, describing the image and what it depicts.You perform a Bradford assay to determine the concentration of isolated α-lactalbumin. You use 50 μL of a two-fold diluted solution of α-lactalbumin in the assay. You generate a standard curve with the following equation for the line: y = 0.163x + 0.082. The absorbance of your sample was 0.674 AU. What is the concentration of α-lactalbumin, in mg/mL, in your sample? Give your answer to three significant figures.You are running a size exclusion column to purify your 25 kDa protein from a lysate mixture. The void volume for the column is 10 mL, while the elution volume is 50 mL.The resin is used to separate proteins from 10 kDa up to 100 kDa.After running 75 mL of buffer through the column, you stop and run samples on an SDS-PAGE gel on fractions that showed absorbance values at 280 nm.On your SDS-PAGE gel, none of lanes shows a band at 25 kDa. What is the best possible explanation for the results? y. Your elution buffer did not have a high enough salt concentration to elute your protein. z. Your protein is not globular so runs at a different molecular weight on the SDS-PAGE gel. aa. You did not run enough buffer through the column to elute your protein. bb. Your protein does not absorb at 280 nm due to no solvent exposed aromatic groups.