Laemmli buffer, also referred to as SDS-reducing buffer, is added to each of the samples. It is a blue solution and the recipe for 2X Laemmli buffer is: 0.125 M Tris HCl, pH 6.8, 20% glycerol, 4% SDS and 10% β-mercaptoethanol (βME). What is the purpose of each of these ingredients?
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Laemmli buffer, also referred to as SDS-reducing buffer, is added to each of the samples. It is a blue solution and the recipe for 2X Laemmli buffer is: 0.125 M Tris HCl, pH 6.8, 20% glycerol, 4% SDS and 10% β-mercaptoethanol (βME). What is the purpose of each of these ingredients?
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- The following stock solutions are available to make a protein extraction buffer: 100% Nonidet P-40, 1 M Tris-Cl, and 0.5 M EDTA. What quantity of the original stocks will be needed to make 250 ml of buffer with the following final concentrations: 0.5% Nonidet, 150 mM Tris-Cl, and 10 mM EDTA?How many mL of the 1 M glucose stock solution do you need to prepare 100 mL of a 1 mM glucose solution?N-(2-hydroxyethyl)piperazine-N'-(2-ethanesulfonic A purified protein is in a Hepes acid) buffer at pH 7 with 375 mM NaCl. A dialysis membrane tube holds a 2.0 mL sample of the protein solution. The sample tube floats in a beaker containing 1.00 L of the same Hepes buffer, but with 0 mM NaCl, for dialysis. Small molecules and ions (such as Na+, Cl-, and Hepes) can to diffuse across the dialysis membrane, but the protein cannot. Assume there are no sample volume changes during the dialysis. Calculate the final concentration of NaCl in the protein sample once the dialysis has come to equilibrium. Calculate the final NaCl concentration in the 2.0 mL protein sample after dialysis in 150 mL of the same Hepes buffer, with 0 mM NaCl, twice in succession. [NaCl] after a single dialysis: [NaCl] after a double dialysis: mM mM
- The 3 proteins have the following properties. Which is the correct order of steps to extract them? + ethyl acetate, + (NH4)2SO4 at 20% saturation, centrifugation, + detergent (Triton X), buffer the lysate (pH=10), centrifugation, collect precipitate + ethyl acetate, + detergent (Triton X), + (NH4)2SO4 at 20% saturation, centrifugation, buffer the lysate (pH=10), centrifugation, collect precipitate + 1 M NaCl, + detergent (sodium dodecyI suIfate), centrifugation, +(NH4)2SO4 at 60% saturation, buffer at pH 7, centrifugation, collect precipitate + ethyl acetate, adjust pH to 7.3, centrifugation, collect supernate, +detergent (Triton X) to precipitate, +(NH4)2SO4 at 30% saturation, centrifugation, collect precipitateAn amino acid mixture consisting of lysine, leucine, and glutamic acid is to be separated by ion-exchange chromatography, using a cationexchange resin at pH 3.5, with the eluting buffer at the same pH. Which of these amino acids will be eluted from the column first? Will any other treatment be needed to elute one of these amino acids from the column?An amino acid mixture consisting of lysine,leucine, and glutamic acid is to be separated by ion-exchangechromatography, using a cation-exchange resin at pH 3.5, with theeluting buffer at the same pH. Which of these amino acids will beeluted from the column first? Will any other treatment be neededto elute one of these amino acids from the column?
- In an experiment, separation of albumin from chicken liver was attempted at 31%, 58%, and 65% saturation with ammonium sulfate, (NH4)2SO4. After homogenization and centrifugation, 23 ml of the supernatant was obtained. What is the volume of saturated buffered (NH4)2SO4 (pH 7.0) that must be added to make the solution 31% saturated? 10.3 ml 8.33 ml 9.50 ml O 12.2 mlStreptomycin sulfate 400 mg IM daily is ordered for a child weighing 77lbs. The recommended dosage is 20-40 mg/kg/day once daily. A 1 gram vial of streptomycin sulfate is available in powdered form with the following instructions: Dilution with 1.8 mL of sterile water will yield 400mg per mL. If safe, how many mLs will you give?N-(2-hydroxyethyl)piperazine-N'-(2-ethanesulfonic acid) buffer at pH 7 with 400 mM NaCl. A A purified protein is in a Hepes dialysis membrane tube holds a 5.0 mL sample of the protein solution. The sample tube floats in a beaker containing 0.50 L of the same Hepes buffer, but with 0 mM NaCl, for dialysis. Small molecules and ions (such as Na*, CI", and Hepes) can to diffuse across the dialysis membrane, but the protein cannot. Assume there are no sample volume changes during the dialysis. Calculate the final concentration of NaCl in the protein sample once the dialysis has come to equilibrium. Calculate the final NaCl concentration in the 5.0 mL protein sample after dialysis in 300 mL of the same Hepes buffer, with 0 mM NaCl, twice in succession. [NaCl] after a single dialysis: [NaCl] after a double dialysis: mM mM
- It is possible to make a buffer that functions well near pH7 using citric acid, which contains only carboxylate groups. Explain.A mixture of lipids containing phosphatidic acid, cholesterol, testosterone, phosphatidylserine, andphosphatidylethanolamine was applied to a hydrophobic interaction chromatography column. Thecolumn was washed with a high salt buffer, and the lipids were then eluted with decreasing saltconcentrations. In what order would the lipids be eluted from the column? Explain your answer.You need to make a protein buffer of: . • • 100 mM NaCl 25 mM Tris 8 5% w/v glycerol • 2 mM DTT Your stock solutions are: 5 M NaCl • 2 M Tris 8 • 70% w/v glycerol • DTT @ 154.25 g/mol How would you make a 1L protein buffer Solution? Show your work and describe.