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type so i can read it please A procedure used to purify your desired protein from Drosophila is presented below: Activity (units Protein mg) 2.936

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A procedure used to purify your desired protein from Drosophila is presented below: Activity (units Protein mg) 2.936 1.041 12 27.028 22.846 10314 Step Homogenate 100,000 sediment Toloene-trypsin treatment and ammonium sulfate precipitation (40-100 DEAE Sephadex G-200 Peak Peak II 4 10.118 13 0.96 4185 2.137 a. Calculate the specific activity for the Sephadex G-200 steps. Which peak (or 1 has the highest specific activity? b. Calculate the percent yield of the final product based on the initial enzyme quantity Calculate the fold increase in purification for each step. d. Assume that the protein is pure after altration chromatography Sephatex G-2001 What percentage of the wa extract contained your protein The purification graph for the DEAE step is shown below 2010 CI AM 2014 The purification for the DEAE step is shown below 09 30 101 300 401 350 OVO 10.00 Proteolytic activy tuniti/mior protein g/m INICI) 2001 000 004 1001 oo A 100 20 300 300 Elutun wol (ml) The conductivity is represented by the dotted line, while the protein concentration in ug/ml) is shown by the closed circles and the proteolytic activity in units/ml) is shown by the open circles. e. Which of the clution peaks is the best peak to select for further purification? Why? The purification graph for the Sephadex G-200 step is shown below. Peas Peak 11 The purification graph for the Sephadex G-200 step is shown below: Peak 1 Peak II 600 500 200 400 160 120 Proteolytic activity (units/ml) 300 M Proteinl (ug/ml) 80 200 40 100 T o 40 60 BO Elution vol. (ml) The protein concentration (in ug/ml) is shown by the closed circles and the proteolytic activity (in units/ml) is shown by the open circles. f. Do these results match with your conclusion from question (a)? Why or why not

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