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- Prior to subculture, Tifa used a hemocytometer to count her HepG2 cells cultured on a T-25 flask. After trypsinization, she prepared her cells by mixing 50 µL of the cell suspension with 50 μL of 0.4% trypan blue. Her observation under the microscope is as shown below: 1 (1) (ii) 3 (iii) 2 (iv) 4 Note: Count cells on the four labelled squares. Include cells touching the line on top and left. 18P 06. ¿66 Ⓡ Determine the number of viable and dead cells from her observation. What is the percentage of viability of this culture? Show your calculations in detail. Calculate the concentration of viable cells per mL in the original culture. Show your calculations in detail. Based on your understanding of cell culture, do you think she should proceed with subculture? Justify your answer.After doing the preliminary studies on redcrest protein extract, Tighnari proceeded with its characterization and analysis proper. He purified the crude protein extract through ammonium sulfate precipitation (40-60%) and gel filtration chromatography. Shown below are the results of the analyses. ||||| 250 kDa Crude Protein Extract 200 kDa 100 kDa 80 kDa 40 kDa 20 kDa ||| || Partially Purified Protein Extract Purified Protein Extract Figure D.1. Electrophoretogram obtained after NATIVE PAGE of the provided protein extracts. PAGE Analysis: 1. Based on Figure D.1., the series of purification procedures led to the isolation of two major redcrest proteins, COL and LEI. Determine the molecular weight of COL and LEI if the results of GFC showed that COL eluted out of the column first.When the yeast cells have completely re-hydrated, measure out 1.8 mL of well-mixed yeast suspension (0.2% yeast) into each of two new 15 mL centrifuge tubes. Add 200 μL of a 10% (w/v) Sodium Azide*** in YGM solution to one of the 15 mL tubes with yeast suspension. Add 200 μl of YGM to the other 15 mL tube of yeast suspension for your Control. Let both tubes incubate at room temperature for 30 min, vortexing every ~5 minutes What is the % concentration of azide in this sample during metabolic inhibition?What is the % concentration of yeast in this sample during metabolic inhibition?
- How would you make two-fold serial dilutions such that the last tube is a 1:32 dilution of the original, concentrated material? Assume that you need to have at least 500 µl of each dilution, and you should be able to perform the dilutions in microfuge tubes with a maximum capacity of 1.5 ml.in a clean, non-sterile 15 mL centrifuge tube, prepare a 2.0% yeast suspension by adding 0.06 g Saccharomyces cerevisiae to 3 mL yeast growing medium (56 mM glucose, 20 mM HEPES, pH 6.8). What percent of yeast suspension is left after a 1:10 dilution?You have an order for 1 gram of Cefazolin in D5W 100 ml. You have added 5 ml of sterile water to the 1 gram vial to reconstitute powder. However the recommended manufacturer’s diluent amount is 10 ml of sterile water for a final concentration of 100 mg/ml. How would reconstituting the vial with 5 mls affect the concentration and the final calculated dose?
- Assume that you are adding 300 microliters of 1% substrate solution per well in a 24-well plate. If we can order 5 milligrams of fibronectin for $871.00, how much would it cost to have enough to use every well of the 24-well culture plate?what is the effect and rationale when three milliliters instead of 1 mL was placed in the Petri dish in pour-plate method?Aspergillus can be used to produce α-amylase (α-AM), which is an enzyme that hydrolyzes the glycosidic bonds in starch molecules into maltose (disaccharide). Pure α-AM has a specific activity of 56.00 U/mg. The α-AM is secreted into the culture media during production (after 5 days, production is complete). Following, the Aspergilluscells are separated by centrifugation and discarded. The culture supernatant (with α-AM) is filtered giving a clarified supernatant with a volume of 100.0 L, activity of 3.00 U/mL, and total protein concentration of 0.650 mg/mL. After purification, the product stream (7.50 L) contains α-AM (25.00 U/mL) and a total of 6.788 x 103 mg total protein. Calculate the following: Concentration of total protein (g/L) and total units of activity in the clarified supernatant and purification product stream. Specific activities (U/g) of the clarified supernatant and purification product stream. Consider significant figures in your answers (may want to use scientific…