BIO 340 Activity #5 Spring A 2024

71.-72. Which variables were kept constant in the experiment? * - The following are the results: Group A Group B 18 cm tall 32 cm tal Treatment: 200 mL of plain water twice 200 mL of fertilizer solution a week for 3 weeks Treatment: twice a week for 3 weeks Your answer

A flat (not spherical) tissue engineered skin (thickness 2.5 mm) is attached to the bottom of a dish and cultured with cell media atop it (which has an oxygen concentration of 0.15 mol/m3). The diffusivity of oxygen in the skin is 3.4 E-9 m2/s, and according to experiments that you’ve performed, you want to make sure that the concentration of oxygen in the device doesn’t fall below 0.06 mol/m3. (Below that concentration harms the cells.) The rate of oxygen consumption is -5.9 E-17 mol/[cell◦s]. What is the maximum cellularity (in cells/mL, three significant digits) that this tissue engineered skin can support?

567write true if the statement is correct, otherwise, change the underlined word/phrase to make it correct. do not use abbreviations please answer all

Please solve both parts in one hour

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Thank ypu very much for your assistance as it is greatly appreciated.

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What is the Posner task? Describe its purpose and setup (materials, conditions, etc.). What do its results (graph pictured here) indicate, and why? Reaction time (msec) 300 250 200 Invalid Neutral Valid Cue

73.-74. Which variable was manipulated in the experiment? * - The following are the results: Group A Group B 18 cm tall 32 cm tal Treatment: 200 mL of plain water twice 200 ml of fertilizer solution a week for 3 weeks Treatment: twice a week for 3 weeks Your answer

Figure 3: ● ● ● ● ● ● KDa ● 97.4 66.2 45.0 ● 31.0- 21.5 14.4 S-1 p-1 S-2 2-0 This figure was generated by centrifuging a pura sample of protein, removing the supernatant, and resuspending the pellet in the same volume as the supernatant to allow direct comparison. The supernatant and pellet samples were then prepared for SDS-PAGE identically and run via normal SDS-PAGE procedures. In the figure, "s" means supernatant and "p" means pellet. The text or number after the dash represents a different condition. For example, s-1 and p-1 are the supernatant and pellet samples under condition 1. It is not shown, but under wild-type conditions, essentially all of the protein is found in the supernatant. S-3 ● What does the intensity of each band represent? ● Would you find soluble protein in the supernatant or pellet? Why? Would you find aggregated protein in the supernatant or pellet? Why? For each condition (there are 5 different conditions), is there a higher percentage of the total protein…

I need help calculating the “Activity ([PNPP]) for each Supernatent. I need to know how to solve this so I can fill out my purification table worksheet. Please help. This class is Biochemistry 1 Lab.

Concentrations in biochemical systems are often very dilute. Consequently, scientific notation and logarithms are often used to express concentrations. In scientific notation, numbers are expressed as coefficient x 10" To convert a number to scientific notation, proceed as follows: 1. Move the decimal place so that there is one digit in front of the decimal. 2. Account for the moved decimal in the value of x. If the decimal moved to the right, x is negative; if it moved to the left, x is positive. A logarithm is basically an exponent. Unless otherwise indicated, a logarithm is the a of 10". The numbers after the decimal point are significant; the number before the decimal just identify the location of the decimal point for the number. Notice that it is easy to estimate a logarithm from scientific notation; it's the exponent! Logarithms are commonly used to express the concentration of H. The pH is defined as pH= log (In), where the base number is 2.303. The same general rules as logs…

1 pt pt 9146 Bb 9146 Bb 1031 Class Etsy E Traps E Traps New Free Chat + ☆ 出口 keAssignment/takeCovalentActivity.do?locator-assignment-take [References] You do an enzyme kinetic experiment and calculate a Vmax of 118 μmol per minute. If each assay used 0.10 mL of an enzyme solution that had a concentration of 0.20 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol? (Enter your answer to two significant figures.) turnover number = sec-1 D 1 pt Submit Answer Try Another Version 2 item attempts remaining estion stion 5 on 6 7 1pt 1 pt 1 pt 1pt 1pt 1pt 1 pt 1 pt D is the substrate concentration multiplied by the catalytic constant. KM is equivalent to the substrate concentration multiplied by the ratio of rate constants for the formation and dissociation of the enzyme-substrate complex. KM is equivalent to the substrate concentration. KM is equivalent to the substrate concentration divided by 2 A: KM is equivalent to the substrate concentration…

PLEASE SHOW COMPLETE SOLUTION.

Discuss the advantage and disadvantage of Wijs method of iodine value determination.

me Lab Evidence-Bas X NC Grades for Beatrice Pierre: 2024 X ourses/192624/quizzes/1488062/take Question 1 Background: While completing the enzyme lab exercises, you learned about the enzyme called catalase, which catalyzes the decomposition of H₂O2 hydrogen peroxide to O₂ (oxygen) and H₂O (water). You have performed experiments to investigate the effect of the following three conditions Substrate concentration, temperature, and pH. During the lab, you generated data, graphed your results, and made general statements about your results. Drawing Evidence-Based Conclusions: Write an overall evidenced-based conclusion about catalase that answers the question below. Your response should include supporting evidence from all of your data (3-4 sentences). Edit View Insert Format Tools Table B I U b My Questions | bartleby What effect did substrate concentration, temperature, and pH have on the activity of catalase? 12pt 3 pts Q Sea Paragraph x

Materials - 2021FA-CHM-1O X Bb 4427577 d-fleet02-xythos.content.blackboardcdn.com/6086c260d7e8f/4427577?X-Blackboard-Expiration=1633143600000&X-Blackboard-Sig 6 / 9 100% Exercise 1: Standard Curve for Protein Measurements: A standard curve for protein concentration is often created using known concentrations of bovine serum albumin (protein). This process is called the Bradford Assay; it is a colorimetric assay. A special reagent turns blue when it binds to amino acids present in protein. The intensity of the color is best measured with a spectrophotometer (a device for comparing two light radiations, wavelength by wavelength). In the case of the Bradford Assay the greater the absorbance, the higher the protein concentration. A series of tests were performed on some samples and spectrophotometer: following measurements were obtained using a Protein Concentration (mg/ml) Absorbance (A) 0.26 0.098 0.56 0.213 0.383 0.84 1.12 0.473 1.40 0.527 TASKS: 1. Enter the data into Excel - the…

Please answer the pKa Values and Identity of Lysine

Name some techniques/approaches (name, describe the major steps, how to analyze/interpret results)  that can be used to satisfy the following requirements:  1. Show that substance is pure protein 2. Only one protein was extracted

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Consider the following set of data and answer the fo

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Explain why each of the following measurements is or is not the result of a Bernoulli trial: (a) The number of surgical procedures performed in a hospital in a week(b) A hospital patient’s temperature in degrees Celsius(c) A hospital patient’s vital signs recorded as normal or not normal

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, caleulate the specific activity of the enzyme after each purification procedure. (b) Which of the purification procedures used for this enzyme is most effective? (c) Which of the purification procedures is least effective? (d) Is there any indication based on the results shown in the table that the enzyme after step 6 is now pure? (e) What else could be done to estimate the purity of the enzyme preparation?

Please answer  a and b both

If the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme inhibitor is inhibitor reversible or irreversible? And why?

Case Study At 1830, 2 men break into the house of a store manager, while the family is having dinner. The wife is taken as a hostage and taken by the intruders, who demand that the husband go to the safe of the business and take out the day's proceeds--probably about $25,000.00. The plot goes badly, the money is never transferred, and the woman is found dead in a field the next afternoon at about 1600. Autopsy shows the stomach to be full of partly digested food material. The question arises as to time of death. The physical findings indicate death about 8 hours previously, and, in fact, a subsequent witness reports he saw her alive in the van at about 0700 that same morning. What factors may account for the food material which showed little evidence of digestion, and no evidence of gastric emptying? What is the potential for error if physiological variation from 'normal' are not taken into consideration?

Can you please help me to complete step by step the Log molecular weight I will appreciate your help

Why are DG°' values not rigorously applicable to biochemical systems?

Question 1: Suppose you have given 5 tablets weighing 449mg, 450mg, 448mg, 451mg and 453mg, respectively. Calculate 300 mg equivalent sample weight for assay. The product claim is 500 mg Vitamin C is present in each tablet. Question 2: Volume of the standard sodium edetate is 12.6 mL (calculated after the assay of Zinc Sulfate Syrup). Determine the % of potency of the drug considering the claimed dose is 11.5

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.

Activity 1 Activity 2 Activity 3 Activity 4

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…