n a pUC19 digest for 1 ug of pUC19 (DNA conc. 282ng/ul) using 10X Cutsmart buffer, pure water and BamHI enzyme in a total volume of 40 ul, how much of each solution is added to the total volume?
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In a pUC19 digest for 1 ug of pUC19 (DNA conc. 282ng/ul) using 10X Cutsmart buffer, pure water and BamHI enzyme in a total volume of 40 ul, how much of each solution is added to the total volume?
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- The diffusivity of amino acids in polyacrylamide gel is approximately 1x10^-9 cm2./s calculate the initial flux of amino acids, give an instantaneous gradient of (20g/cm 3 )/8cm Why is polyacrylamide gel is used in electrophoresis?A series of standard proteins and an unknown enzyme were studied by gel filtration on a Sephadex G200 (the 200 refers to the maximum pore size in kDa) column. The elution volume Vel for each protein is given in Table 1 below. (a) Plot the data in the form of log Mr versus elution volume. From the line of best fit through the points for the standards, determine the Mr of the unknown enzyme. Explain why ferritin and ovomucoid behave anomalously. Table 1 - The Vel versus Mr data Protein Mr Vel (mL) Blue dextran* Lysozyme Chymotrypsin Ovalbumin Serum albumin Aldolase Urease Ferritin# Ovomucoid# Unknown 1,000,000 14,000 25,000 45,000 68,500 150,000 500,000 700,000 28,000 ⎯ 85 200 190 170 150 125 90 92 160 139 *Blue dextran is not a protein but a high-Mr carbohydrate that has a covalently bound blue dye, and it elutes with the void volume of the column. # Do not…A solution containing egg albumin (pl=4.6), B-lactoglobulin (pl=5.2), and chymotrypsinogen (pl=9.5) was loaded onto a column of diethylaminoethyl cellulose (DEAE-cellulose) at pH 5.4.The column was then eluted with a pH 5.4 buffer, with an increasing salt concentration. Predict the elution pattern.
- 1. Lactoferrin is an iron-binding glycoprotein that forms the antibiotic fragment lactoferricin during digestion. The protein was isolated from 1.5 liters of ewe skim milk by successive ammonium sulfate precipitation until a final salt concentration of 70% was obtained. Determine the amount (in g) of powdered ammonium sulfate needed in bringing the solution from (a) 0% to 40% saturation and (b) 40% to 70% saturation assuming that the volume remains constant. Initial concentration of (NH4)2SO4, % saturation 0 10 20 30 40 50 60 70 80 90 10 55 Final concentration of (NH4)2SO4, % saturation 30 40 50 60 70 80 Grams of solid (NH4)2SO4 to be added to 1 L of solution 176 242 314 390 472 561 657 117 405 491 584 59 421 351 438 20 113 57 182 121 61 251 325 63 188 126 195 130 65 260 337 270 202 281 135 67 210 140 70 90 761 685 511 609 533 365 292 219 146 HUGH LATLE 100 73 457 381 305 228 152 76If the absorbance at540nm of a biuret and protein solution containing 0.25mg/ml of protein .24 the absorbance of a biuret and protein and dna solution containing.25mg/ml of protein and 0.5mg/ml dna should be note the total volume is the same in both solutions 0.24 0.72 0.48 not enough inforFrom this standard curve and chart below, does the separation of molecules in the mixture appear successful from the gel filtration? Is there a clearlydefined separation between molecules? Explain your conclusions. Parameters required for calculation of coefficient (Kd) for unknown protein Volume eluted (mL) Which variable does this volume represent in the equation for Kd? Fraction with maximal DNP-Aspartate detected 36 Vt Fraction with maximal Protein detected 24 Ve Fraction with maximal Blue dextran detected 6 Vo
- 13. 0.9% (m/v) NaCI solution and 5% (m/v) glucose solution are both isotonic to red blood cells. SHOW your work and watch sig figs & units. c. convert the concentration from M to % (m/v) for a 0.342 M NaC solution. (HINT: convert to g/ml and then multiple by 100%)An allosteric enzyme is purified and determination of its mass by gel-filtration chromatography yields 240 kDa. Chromatography in the presence of 6M urea yields a 30 kDa species and 90 kDa species. SDS-PAGE in the presence of Beta mercaptoethanol reveals 2 protein bands of 30 kDa and 45kDa. Describe the quatranary structure.Which of the following is NOT a unit of concentration? All of these options are units of concentration. mM Moles/Liter Molar You gathered your data from Lab , and found the following values: Total Activity of lysozyme in HEW: 14 units Total Activity of lysozyme in carb 1: 21 units Total amount of protein in HEW: 70 mg Total amount of protein in Carb 1: 15 mg Calculate the extent of purification of lysozyme in Carb 1. A 7 fold B 150% C 15 fold D 70%
- To prepare a gel sample, you want to load 50 ng total of protein/well. You have added 200 μL of protein in 800 µL reagent and measured your sample by Bradford A595 to be 0.7 mg/mL - your dilution is unaccounted for at this point. Assuming a total final volume of 20 μL, what volume of protein sample, buffer and 4X SDS PAGE Loading Dye needs to be mixed to create a final sample of 50 ng protein in 20 μL?A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).suctose density gradient ultractifugation is a powerful technique for fractionating macromolecules like DNA,RNA and proteins.some protocols using sucrose gradients mention the following:10 mL sucrose gradients 10-15%(w/v) in 10 mM HEPES buffer.How would you prepare this sucros gradient?