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- Agarose gels can vary from 0.8 to 2% explain why we use different gel percentagesWe’re back in the lab having fun! Our current experiment calls for us to treat our cells with THC (yeet!, delta 8 from hemp of course lol) and the final concentration of 15 µM once it has been added to the cells. We need to treat 10 mL of cells, and we don't want our treatment volume to be more than 10 µL per 1 mL of cells. What concentration should we make our stock solution? (I submitted this question before and got an answer of 150 µM and that was incorrect)Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) 1. Why do you destain the gel? 2. What is a gradient gel? Why are we using them? 3. Compare and contrast SDS-PAGE and native PAGE. Why would we want to do each of these techniques?
- You have a sample at 50 ng/ul and you would like to load 400ng of this sample on a lane of an agarose gel. You also have TE buffer as diluent and 6x loading dye. Your total sample should be 12ul. Calculate the amounts of each reagent necessary to prepare this sample for gel loading.50 mg/50 ml kinetin stock is available You need 2.5 mg/l kn for Ms media calculate amount of kn is required? Explain the role of surface sterilising chemicals in aseptic culture initiation and function of sucrose in MS medium?1. Isoelectric focusing. A digested protein sample was applied to one end of a gel strip with an immobilized pH gradient. According to the experimental image from the results by gel running. Please indicated that what amino acids were compositionally enriched in separated dot 1 and 2? pH 9 Dot An electric field is applied Dot Decreasing pl pH 3 After staining, proteins are shown to be distributed along pH gradient according to their pl values.
- Example of a Protein Purification Scheme: Purification of the Enzyme Xanthine Dehydrogenase from a Fungus Volume Total Total Specific Percent Fraction (mL) Protein (mg) Activity Activity Recovery 1. Crude extract 2. Salt precipitate 3. Ion-exchange chromatography |4. Molecular-sieve chromatography 5. Immunoaffinity chromatography 3,800 22,800 2,460 0.108 100 165 2,800 1,190 0.425 48 65 100 720 7.2 29 40 14.5 23 1.8 275 152.108 11 Calculate the specific activity of step#4. Note that percent recovery=% Yield.Wh are doing this procedures can you explain? (ex. heating or adding chemicals etc.) 1) Purification of Vitelline from Egg Yolk-Experimental ProcedureMeasure the volume of 3 egg yolks and mix by adding an equal volume of NaCl solution.Extract the mixture with 3-fold volumes of ether and separate the aqueous phase.Do the same procedure 3 times.Mix the sample with water and rinse.It is expected for the protein to collapse.Some more water is added in order to check whether the collapse occurs completely.The sample is centrifuged and the precipitate is dried. 2) Purification of Plasma Albumin and Fibrinogen-Experimental ProcedureAdd ammonium sulfate to 10 ml plasma up to 25% saturation.Separate the collapsed fibrinogen by centrifuge.Increase the saturation level to 33% by adding (NH4) 2SO4.Separate the globulin by centrifugation.Separate prodoglobulins by increasing the saturation level to 46%.Increase the saturation level up to 64% to precipitate albumin.Separate the albumin by centrifuge…PROTEINS 1. What will happen to free arginine after being subjected to biuret analysis (is it positive or negative, include color)2. What will happen to beef extract after being subjected to ninhydrin analysis (is it positive or negative, include color)
- 100ml of LB media with 25 μg/ml of Amp and 100 μg/ml of Kan final concentration. You have 100ml of LB provided and Amp and Kan stocks at 100 mg/ml and 50 mg/ml provided. Determine how much of each antibiotic stock solution you need to add to 100ml of LB to reach desired antibiotic concentration.Standard curves You are setting up a standard curve for lysozyme. You have a stock vial containing 2 mg/ml of lysozyme and you have 2 ml in the vial. You will want to have a minimum of 1 ml of each concentration for the spectrophotometer. How would you proceed? (Saline is added to make the various concentrations). Concentration Am't stock lysozyme or am't of a previous dilution (note which) Amount saline Total volume wanted 1.00 mg/ml 0.75 mg/ml 0.50 mg/ml 0.375 mg/mlOops! Your pipettor wasn’t set correctly and you only pipetted 87 µl of a 10-7 dilution when plating serial dilutions. But, you noted this error in your lab notebook so you could correctly perform the calculation. When this plate was grown, you counted 147 colonies on the plate. What was the concentration of bacteria in the original, undiluted suspension?