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- Which stationary phase is better in separation of the components of moringa extract for column chromatography? Sodium Bicarbonate or Silica Gel? And Explain.What is optical density (OD) and how is it measured? How is it related to the concentration of the analyte? And what is a colorimetric assay?The original concentration in a sample of kombucha is 2.79 x 10^6 CFU/ml. Which dilution would yield a countable plate? How would you make this? Show your calculations. Confused as to what's implied by "which dilution"? does it mean, how many times?
- 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.1) You have been asked to make up four 1.5% agarose gels at 30 ml each. Ethidium Bromide is to be added at 0.5 ug/ml and you have a bottle at 10ug/ml. Write down step-by-step protocol of how to proceed. 2. How would you make up one liter of 1X TAE buffer using a 25X stock?If you have 50 ml of pure stock formalin solution how many ml of diluent will you need? What is the total volume of the reagent used you have prepared? Write down your answers with complete solutions and correct labels.
- 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.What is the fluid thioglycollate medium? Please explain the testing and its results and the chemistry behind it?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. ||||| 250 kDa Crude Protein Extract 200 kDa 100 kDa 80 kDa 40 kDa 20 kDa ||| || Partially Purified Protein Extract Purified Protein Extract Figure D.1. Electrophoretogram obtained after NATIVE PAGE of the provided protein extracts. PAGE Analysis: 1. Based on Figure D.1., the series of purification procedures led to the isolation of two major redcrest proteins, COL and LEI. Determine the molecular weight of COL and LEI if the results of GFC showed that COL eluted out of the column first.