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- 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.Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE)1. What are the functions of the sample buffer and sample reducing agent? Why do the samples need to be heated before you load them on the gel?2. What determines the current in your gel? What could cause the current in your gel unit to be lower than expected? Is there anything that could cause it to be higher than expected?3. Why do you need to wash the gel before staining it? Why use warm water?1- Are the following changes in conditions likely to increase or decrease retention time? a. faster flow rate b. longer column c. longer connector between column and detector d. higher analyte concentration e. higher temperature f. larger sample size g. using a less polar column while doing a reverse-phase separation h. using a less polar mobile phase while doing a reverse-phase separation 2- In what order will the following substances elute? • In reverse-phase liquid chromatography: a. butylamine, 2-butylene, ethylamine, ethylene b. benzene, chlorophenol, phenol, trichlorophenol • In gas chromatography with a polar column: c. butanol, methanol, water • In gas chromatography with a nonpolar column: d. butanol, methanol, water • In ion chromatography: e. bromide, fluoride, sulfide
- Hi, I just need some help calculating the final concentration for each of the standard solutions I made. The concentration of my stock solution is 0.1mM.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?Now prepare a 500 ml media having ¼ strength MS with 5mM BAP, 5.5 mg/l Kn and coconut water 10%. Stocks are MS Macro 10X, micro 20X, FeEDTA 10X, Organic 100X, BAP and Kn 5gm/100ml. If you need anything else then you add accordingly. BAP has a MW of 225.3. Sucrose and Myo-inositol is not mentioned in the question. These you need to add. Consistency of the medium is also mentioned.
- You have a 50X stock solution of TAE buffer, but you need 2 L of a 1X solution for electrophoresis. How much stock should you use?2. Provide a one-sentence broad generalization regarding the % acrylamide one should use in SDS PAGE gels and the MW range targeted. 3. Name and give the purpose of each component in the electrophoresis buffer (specify type and pH) used for SDS PAGE.4. What total dilution would you need to a 2 uM sample from a 50 mM stock solution? 5. Propose a dilution scheme (simple or serial, as appropriate) for preparing the total dilution you calculated in problem 4.
- 2. For the serial dilution, your stock solution must have a concentration of 3.5 mg/mL. How much diluent must be added to the 5.3 mg/mL red cell to prepare the stock solution? Show pertinent solution/s. How much of the diluent must be added to tube 2 if 200uL Red cell suspension is added? Show pertinent solutions. What are the initial concentrations used for tubes 3, 5, and 6? Show pertinent solutions.7. A total of 7.21 g of dry mixture with a protein content of 89.2% (w/w) determined by Kjeldahl analysis was dissolved in 88.54 g of sterile water and centrifuged to purify the protein in the mixture. After centrifugation, a total of 5.95 g of precipitated pellet was formed, and the protein content in pellet was determined as 72.2% by spectrophotometric Lowry analysis. Assume that pellet is not a hygroscopic material and does not absorb any water. Determine the following: a. the protein concentration in the supernatant layer after centrifugation in % w/w b. the nature of amino acids in the protein structure. What's the possible explanation?Large proteins travel/migrate faster in both gel filtration chromatography and SDS- PAGE. O True O False