4.Was it appropriate to use human serum protein as the standard when you wereanalyzing egg proteins in your unknowns? Explain.

When analyzing egg proteins in unknown samples, using human serum protein as a standard may not be…

Answered: Was it appropriate to use human serum…

Essentials Health Info Management Principles/Practices

4th Edition

ISBN:9780357191651

Author:Bowie

Publisher:Bowie

Chapter7: Numbering & Filing Systems And Record Storage & Circulation

Section: Chapter Questions

Problem 3CR

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2. Suppose you prepared the following six test tubes as indicated in the table below. You divide the material in each tube appropriately into two separate tubes, and pro- ceed to run an orcinol and a diphenylamine test. Tabulate and explain the results you would expect to obtain from the Six orcinol tests and the SIX diphenylamine tests. Reagent DNA (m1) RNA (ml) Water (m1) 0.5 N KOH (ml) 10% TCA (m1) 1 2 ININ 2 2 2 2 1 Test Tube Number 3 4 2 2 2 2 5 2 NIN 2 6 2 2
1. What are the three general steps involved in isolation of proteins? Discuss or briefly describe the purpose of each step. 2. Suggest a simple procedure (or test) to verify if the final product is indeed casein.
1. What is the function of each step or reagent used in the isolation of casein from milk? Reagents: a. Warm distilled water b. Vinegar c. Ethanol 2. What are the three general steps involved in the isolation of proteins? Discuss or briefly describe the purpose of each step. 3. Suggest a simple procedure (or test) to verify if the final product you obtained is indeed casein.
2. The following data were generated after a set of bovine serum albumin standards were measured via the BCA assay. Table 1. Absorbance measurements at 562 nm for BSA standards measured in triplicate in a BCA Assay. Standards A B C D E F G H I Conc (ug/ml) 2000 1500 1000 750 500 250 125 25 0 Replicate 1 Abs @ 562 nm 2.381 2.039 1.505 1.143 0.819 0.454 0.245 0.056 0 Replicate 2 Abs @ 562 nm 2.456 2.052 1.489 1.156 0.823 0.46 0.272 0.049 0 Replicate 3 Abs @ 562 nm 2.43 2.05 1.47 1.17 0.81 0.48 0.255 0.053 0.00 Use Excel or your graphing program of choice to create a standard curve using the data from table 1. Consider the best way to graph this data. Make sure the type of graph that you select will allow you to add a line of best fit. Display the equation for the line of best fit directly on the graph. Hint... you'll want to think about how to treat the triplicate values when making the graph. Also consider the type of graph that should be selected to allow for addition of the line of…
6. B. samples A and B in the tubes provided. Tube A B Using the spectrophotometer, perform DNA separation purity analysis of 260:280 ratio Mass of empty tube DI Water 2.80 Which of the samples (Tube A or B) represent values consistent with DNA contaminated with residual substances? Explain your rationale. Mass of water and tube 1.80 7. A. (p) 3 microcentrifuge tubes were labeled and the empty mass was recorded. DI water was added to each tube as noted below. The final mass of the tubes containing the water was recorded. Which tube represents the most inaccurate micropipetting? Tube 1 .280g 5uL .284g Tube 2 .280g 50uL .318g Tube 3 .280g 500uL .780g
7. Will denaturation change the primary sequence of the proteins? Why or why not? 8. Why was distilled water included in the samples tested?
Match the types of data to the example. Precise measurements Assay standard Positive control Quantitative results Negative control Qualitative results Standard curve…
1. The concentration of the glucose stock solution in bottle is 50 µM. This stock solution was diluted by a, factor of 10. If you took 25 ml out of the diluted solution and added it to a new test tube containing the following reagents 5 ml of water, 10 ml of cofactor and 10 ml of buffer. What is the final concentration of glucose in the new test tube?
2. Consider the following paragraph from a peer-reviewed publication detailing the extraction and isolation of a lectin: "30 g of dry S. sclarea seeds were ground in a Waring blender and the meal was stirred overnight in 400 ml of Phosphate Buffered Saline (PBS), at 4 °C. The solution was centrifuged at 20,000 X g for 30 min, and the pellet was re-extracted by mixing with another 400 ml of PBS, overnight at 4°C. The two supernatants were combined and frozen at -20 °C. After thawing, the insoluble material was spun down (3,500 X g for 30 min), and the clear supernatant (crude extract) was precipitated with 50% (v/v) cold ethanol at 4 °C. After centrifugation (20,000 X g for 30 min), the pellet was discarded, and the supernatant was further precipitated with cold ethanol up to 80% (v/v) at 4 °C. After one night in the cold room, the solution was centrifuged (20,000 X g for 30 min), the supernatant was discarded, and the pellet was re-dissolved in water, dialyzed for 3 days at 4 °C…
25. Assume we are performing a 2x serial dilution series of methylene similar to WL-1. If your original, 1x tube is designated "Tube 1", then what would be the relative concentration of methylene blue in Tube 4? a. Tube 4 is the 8x dilution tube. The concentration of methylene blue in this tube is 1/8 that of the original tube. b. Tube 4 is the 8x dilution tube. The concentration of methylene blue in this tube is 8 times that of the original tube. c. Tube 4 is the 4x dilution tube. The concentration of methylene blue in this tube is 4 times that of the original tube. d. Tube 4 is the dilution 10x tube. The concentration of methylene blue in this tube is 1/10 that of the original tube. e. None of the above
2. Consider the following paragraph from a peer-reviewed publication detailing the extraction and isolation of a lectin: "30 g of dry S. sclarea seeds were ground in a Waring blender and the meal was stirred overnight in 400 ml of Phosphate Buffered Saline (PBS), at 4 °C. The solution was centrifuged at 20,000 X g for 30 min, and the pellet was re-extracted by mixing with another 400 ml of PBS, overnight at 4°C. The two supernatants were combined and frozen at -20 °C. After thawing, the insoluble material was spun down (3,500 X g for 30 min), and the clear supernatant (crude extract) was precipitated with 50% (v/v) cold ethanol at 4 °C. After centrifugation (20,000 X g for 30 min), the pellet was discarded, and the supernatant was further precipitated with cold ethanol up to 80% (v/v) at 4 °C. After one night in the cold room, the solution was centrifuged (20,000 X g for 30 min), the supernatant was discarded, and the pellet was re-dissolved in water, dialyzed for 3 days at 4 °C…
A series of bovine serum albumin (BSA) was prepared and 1 mL of each solution was subjected to a Bradford assay. The increase in absorbance at 595 nm relative to the concentration of protein was plotted as shown below. Save 1.0- 0.8- 0.6- 0.4- 0.2- 0.04 0.0 0.5 1.0 2.0 2.5 1.5 BSA concentration (mg/mL) a) Using the graph, calculate the original concentration of protein present in a mixture of haemoglobin and methylene blue (diluted 1:50), which gave an absorbance of 0.20 at a wavelength of 595 nm using the Bradford assay. Show all workings. Absorbance (O.D.)

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