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The correct order of steps when purifying a protein are: Group of answer choices 1)Growing bacterial culture for fusion protein; 2)Harvesting IPTG-induced cultures; 3)Lysing bacterial cell; 4)Removing insoluble debris; 5)Using Affinity Chromatography to purify protein.   1)Growing bacterial culture for fusion protein; 2) Breaking open bacterial cells; 3) Removing insoluble debris: 4) Harvesting IPTG-induced cultures; 5)Using Affinity Chromatography to purify protein   1) Growing bacterial culture for fusion protein; 2) Lysing bacterial cells; 3) Harvesting IPTG-induced cultures; 4) Removing insoluble debris: 5)Purifying protein by affinity chromatography   1)Growing bacterial culture for fusion protein; 2) Removing insoluble debris; 3) Harvesting IPTG-induced cultures; 4)Breaking open bacterial cells; 5)Purifying protein by affinity chromatography

Tabulate the different protein precipitation methods by completing the table below.

colored. Interpretation: () Lactose Observed that the addition of the Benedict reagent to the specimens, the test tube is placed in a 20-minute water bath, in which the sample's color precipitates as a silver- colored. Interpretation: (+) Sucrose With the addition of the benedict reagent to the samples, the test tube is placed in a 20- minute water bath. The color of the sample becomes translucent. Interpretation: (O Starch With the addition of the benedict reagent to the samples, the test tube is placed in a 20- minute water bath. The color of the sample becomes translucent. Interpretation: () This material should not be duplicated nor distributed without permission. BIOCHEM LABORATORY: CARBOHYDRATES GUIDE QUESTIONS: 1. Some of the test(s) you tried from this virtual lab are important basis for determining glucose levels of diabetic patients from blood and/or urine. Can you identify which are these tests and how is modern method used glucose monitoring different? (Show the reactions)

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.

Gel-filtration chromatography is a useful method for removing salts, such as ammonium sulfate, from protein solutions. Describe how such a separation is accomplished.

in isolating ribosomes from a yield sample, describe the ideal type of centrifugation for this separation technique based on the following:*Main type of centrifuge *Subtype centrifuge * Speed range *Operational temperature range*Type of Centrifugation

topic: Isolation of Crude Ovalbumin from Egg White by Ammonium Sulfate Precipitation (Salting Out) Aside from ovalbumin, what are other possible proteins which can be isolated from egg white? Give their biological significance.

Explain how gel filtration chromatography works. What type of gel will you used when the protein size is 2500 Da? Explain.

Besides agarosc gel electrophoresis, there is also SDS-PAGE for separation of macromolccules. Differentiate both these methods.

Give detailed Solution with explanation needed

TRUE OF FALSE: Is E coli colonies would be pink mucoid in Eosin Methylene BlueAgar (EMBA)? Is Coliform colonies would be pink mucoid in Eosin Methylene BlueAgar (EMBA)?

Please complete the table on basis of the categories mentioned.

SDS-PAGE gels are useful in determining the molecular weights of proteins; however, the molecular weights of are usually not reliable. protei

Describe how the following technique work on protein purification? ammonium sulfate precipitation

Given this, if you used 6g of vitamin Z powder to make 20 ml of solution, what is the % concentration of this solution? (I gave the image since I don't know if that info is needed to solve this question.)It also gives a follow-up, if you can help here too: You work in a lab as a summer student. One of your tasks is to make sure that there is enough cell culture medium containing antibiotics to grow bacteria.  One day you realize that there is only 5 ml of 10% Antibiotic stock solution in the freezer. You decide to use it all to prepare the working culture medium with 0.01% antibiotic. In the lab there is plenty of growth medium without antibiotics. (Note: dilution in medium is like dilution in water). You remember the equation to make dilutions of stock solutions. You usually use this formula to calculate the required volume of a stock solution, but you realize it can apply here as well, even though the unknown is the final volume. So, you make that dilution.  Given that each bacterial…

Theoretical Data Following the modified protocol for the isolation of Escherichia coli bacteriophage of Encabo (2018) presented below, compute for the pfu/ml of the chloroform-treated lysate. 1ml 1ml 1ml 1ml 1 Chloroform-treated lysate 1ml Dilution 10-3 10-4 10-5 0 0 0 0 0 9ml 9ml 9ml 10-1 10-² 10-3 Empty sterile tubes Incubate inside ref for 15-20min + 0.1 ml lysate-E.coli mix 0.1 ml 9ml 9ml 104 10.5 // 0.1 ml 0.1 ml +0.5 ml E. coli ↓↓↓↓↓↓ Incubate O/N at 35°C, observe for plaques Molten soft agar overlay B. Quantification of the Infective E. coli other Bacteriophage Particles in the Raw Sewage Sample Volume of Stock Plated (in ml) Bottom agar No. of Plaque-Forming Units (pfu) Ave. A B 254 265 132 110 11 23

Your colleague handed you a novel strain of coli that is purifying a protein with a 6xHisTag; they claim it is superior to the TOP10 cells you have been using. But even with a larger culture size, you discover that your protein yield—using the same Ni-NTA column—is quite low. You discover that the novel strain of Escherichia coli generates an unusually high quantity of dicarboxylic acids, a byproduct of the citric acid cycle that is recognized for its ability to function as an all-purpose metal chelator. What do you think the issue is with purifying IMAC protein with this new strain of E. coli?

What types of macromolecules are usually separated on agarose electrophoresis gels?

Topic: Isolation of E. coli bacteriophage   What would happen if: - the enrichment method in the isolation of bacteriophage was omitted? - the chloroform was not added to the enrichment? - the 0.1 ml lysate-E. coli mix was plated directly on top of the bottom agar?

Please help me with this question. The answer choices are in [ ] If bacteria are killed by an antibiotic, the antibiotic is       ["Bactericidal" OR "Bacteriostatic"]  and we would expect       ["Growth" OR "No Growth"]  on our TSA subculture plates If an antibiotic does not kill the bacteria, but rather the bacterial growth is inhibited, the antibiotic is       ["Bactericidal" OR "Bacteriostatic"]  .  For these types of antibiotics, we would expect       ["Growth" OR "No Growth"]  on our TSA subculture plates in this latter type of antibiotic.

Discuss the functions and components of Biuret dye in protein content determination. Identify two other methods of protein determination and differentiate them from Biuret method. Why is BSA used as standard for protein content determination? Can other proteins be used instead?

TRUE OF FALSE: Is E coli colonies colorless in Eosin Methylene BlueAgar (EMBA)? Coliform colonies colorless in Eosin Methylene BlueAgar (EMBA)?

Compare and contrast the following protein characterization techniques in terms of the principles governing their functions Gel filtration chromatography and isoelectric precipitation

SDS-PAGE reagents that play a role in denaturing the protein sample include (Select all that applies)     Bromophenol blue     APS     Sodium Dodecyl Sulfate     Acetic Acid     Glycerol     Heat     Beta-Mercaptoethanol     TEMED

Compare and contrast the following protein characterization techniques in terms of the principles governing their functions.    size exclusion chromatography vs ion-exchange chromatography

protein is purified and at a concentration of 600 μg in 1.75 ml of buffer. You do an assay with your purified protein, and the assay requires 25 μg of biochemisfunase. What volume of the purified biochemisfunase would yield 25 μg? Show your calculation.

The first choice : ori lacZ blaz araC GFP The second choice : arabinose Ampicillin  X-gal IPTG GFP The third choice : X-gal lactose arabinose GFP Ampicillin The fourth choice : on ice at 42℃ at 95℃ at 37℃ at RT The fifth choice : arabinose ampicillin lactose X-gal GFP