A biochemist discovers and purifies a new enzyme, generating the purification table below. Procedure Total protein (mg) 20,000 5,000 4,000 Activity (units) 4,000,000 3,000,000 1,000,000 800,000 750,000 675,000 1. Crude extract 2. Precipitation (salt) 3. Precipitation (pH) 4. Ion-exchange chromatography 5. Affinity chromatography 6. Size-exclusion chromatography From the information given in the table, calculate the specific activity of the enzyme after each purification procedure. b. Which of the purification procedures used for this enzyme is the most effective (I.e. gives the greatest relative increase in purity)? Which of the purification procedures is least effective? d. Is there any indication based on the results calculated in part A that the enzyme after step 6 is now pure? What else could be done to estimate the purity of the enzyme preparation? 200 50 45 a. C.

A biochemist discovers and purifies a new enzyme, generating the purification table below. Procedure Total protein (mg) 20,000 5,000 4,000 Activity (units) 4,000,000 3,000,000 1,000,000 800,000 750,000 675,000 1. Crude extract 2. Precipitation (salt) 3. Precipitation (pH) 4. Ion-exchange chromatography 5. Affinity chromatography 6. Size-exclusion chromatography From the information given in the table, calculate the specific activity of the enzyme after each purification procedure. b. Which of the purification procedures used for this enzyme is the most effective (I.e. gives the greatest relative increase in purity)? Which of the purification procedures is least effective? d. Is there any indication based on the results calculated in part A that the enzyme after step 6 is now pure? What else could be done to estimate the purity of the enzyme preparation? 200 50 45 a. C.

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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A biochemist discovers and purifies a new enzyme, generating the purification table below. Procedure Total protein (mg)Activity (units) 1. Crude extract 20,000 4,000,000 2. Precipitation (salt) 5,000 3,000,000 3. Precipitation (pH) 4,000 1,000,000 4. lon-exchange chromatography 200 800,000 5. Affinity chromatography 50 750,000 6. Size-exclusion chromatography 45 675,000 (a) From the information given in the table, calculate the specific activity of the enzyme after each purification procedure.
A biochemist discovers and purifies a new enzyme, generating the purification table below. Procedure Total Protein (Mg) Activity (Units) Crude Extract 20,000 4,000,000 Precipitation (Salt) 5,000 3,000,000 Precipitation (pH) 4,000 1,000,000 Ion Exchange Chromatography 200 800,000 Affinity Chromatography 50 750,000 Size-exclusion Chromatography 45 675,000 a) From the information given in the table, calculate the specific activity of the enzymeafter each purification procedure.b) Which of the purification procedures used for this enzyme is most effective (i.e., givesthe greatest relative…
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.
3) Define gel electrophoresis, including its theory and application. Describe the steps of running gel electrophoresis using the following image. More detailed reading: https://www.sciencedirect.com/topics/medicine-and-dentistry/agar-gel-electrophoresis POWER SUPPLY CATHODE ELECTROPHORETIC BUFFER ANODE WELL SAMPLE AGAROSE GEL POWER SUPPLY CATHODE ANOCE HIGH MOLECULAR WEIGHT SPECIES LOW MOLECULAR WEIGHT ANALYTES
The reults for the macroscopic part: 0.30M glycerin – solution was translucent (could see text behind the test tube) 0.15M NaCl – solution was opaque (could not see text behind the test tube) 0.30M NaCl – solution was opaque (could not see text behind the test tube) 0.15M glucose – solution was translucent (could see text behind the test tube) 0.30M glucose – solution was opaque (could not see text behind the test tube) 0.30M Urea – solution was translucent (could see text behind the test tube) Results for microscopic part: 0.30M glycerin – no cells present 0.15M NaCl – normal sized cells 0.30M NaCl – crenated (shrunken and star-shaped) cells 0.15M glucose – no cells present 0.30M glucose – normal sized cells 0.30M Urea – no cells present Determine the osmolarity (hypoosmotic, isosmotic, or hyperosmotic) and tonicity (hypotonic, isotonic, hypertonic) of the following solutions.In which solutions did the osmolarity NOT match the tonicity? For those solutions, why did the osmolarity…
A technician prepares a buffer solution that will be used to facilitate the optimal pH for an enzyme involved in the biotechnological degradation of organic compounds. The buffer compound will facilitate a stable pH. To prepare the buffer they need to determine the required concentration of anita hara [conjugate acid or base]_08 They have been provided with the buffer parameters provided in the images. Provide the answer to three decimal places and include an appropriate unit. Note: You may need to round the numbers to get the required answer. Final volume of solution: 200 ml VEENER Total buffer compound concentration: 150 mM Ratio conjugate base/weak acid: 1.58/1 2000 Concentration weak acid: 0.058 M Final pH of solution: 6.5 Buffer compound pk.: 6.3 14 13 12 11 10 9
Gel-filtration chromatography is a useful method for removing salts, such as ammonium sulfate, from protein solutions. Describe how such a separation is accomplished.
Compare and contrast the following protein characterization techniques in terms of the principles governing their functions. electrosrapy ionization mass spectrometry vs polyacrylamide gel electrophoresis
Since the development of the calcium chloride transformation procedure, other procedures have been developed. One is called electroporation. Using your textbook or other sources, describe this procedure for transformation.
Specificity Specificity is the ability to measure accurately and specifically the analyte of interest in the presence of other components that may be expected to be present in the sample matrix. It is a measure of the degree of interference from such components, as other active ingredients, excipients, impurities, and degradation products, insuring that a peak response is due to a single component only. Experimental Dissolve amount of paracetamol (20 µg/ml) powder in three different volumetric flasks containing IN HCI, IN NaOH and 6% H₂O2 respectively, then keep your solution overnight in a fume hood. Analysis your solution by injecting three times each solution and calculates the recovery% 1 N HCI Peak area Actual exp. conc. Recovery% IN NaOH 6% H₂O2
Your pharmacy has on hand Tetracycline 250 mg/5 mL liquid.You receive a prescription for Tetracycline syrup 500 mg qid for 7 days. How many total milliliters would you dispense? Your pharmacy has on hand Prednisone 5 mg tablets.You receive a prescription for Prednisone 5 mg ii tabs stat and qid x 1 day, then ii tabs tid x 2 days, then ii tabs bid x 2 days, then i tab tid x 3 days, then i tab bid x 3days, then i tab qd x 4 days How many tablets would you dispense for this prescription? How many days will the patient take this medication for? Your pharmacy has on hand Dilantin 100mg capsules.You receive a prescription for Dilantin 100 mg 1 cap po in the AM & PM, 200mg (2 caps) po at noon, and 300mg (3 caps) po at hs. Dispense a 30 day supply. (using the 100mg capsules you have in stock) How many capsules will you dispense? Your pharmacy has on hand Dakins Irrigation Solution 1 liter.You receive a prescription for Dakins Irrigation Solution Irrigate chest tube with 100 mL…
Millon-Nasse Test Mix 1 mL of the sample and 5 drops of Millon-Nasse reagent. Boil the content gently for 30 seconds. Cool in water. Add 2 drops of freshly prepared 1% NaNO2 and warm gently. Observe the color of the precipitate and/or the solution. Question 1. Will all amino acids and proteins give a positive reaction to this test?Question 2. What causes the color of the solution or precipitate?