We graphed the standard curve using the bovine serum protein solution. We then extracted albumin and globulin from egg whites. After getting the absorbance values for our samples, we used the standard curve from the bovine protein data to calculate the unknows of our albumin and globulin concentrations. Was it appropriate to use bovine serum protein as the standard when you were analyzing egg proteins in your unknown? Explain.

We graphed the standard curve using the bovine serum protein solution. We then extracted albumin and globulin from egg whites. After getting the absorbance values for our samples, we used the standard curve from the bovine protein data to calculate the unknows of our albumin and globulin concentrations. Was it appropriate to use bovine serum protein as the standard when you were analyzing egg proteins in your unknown? Explain.

Name: We graphed the standard curve using the bovine serum protein solution.
Uploaded: 2024-03-20T06:42:55.000Z
Channel: Bartleby
Description: We graphed the standard curve using the bovine serum protein solution. We then extracted albumin and globulin from egg whites. After getting the absorbance values for our samples, we used the standard curve from the bovine protein data to calculate t

Curren'S Math For Meds: Dosages & Sol

11th Edition

ISBN:9781305143531

Author:CURREN

Publisher:CURREN

Chapter1: Relative Value, Addition, And Subtraction Of Decimals

Section: Chapter Questions

Problem 27SST

See similar textbooks

Similar questions

A unique aquatic plant was discovered from a lagoon in El Nido, Palawan. To determine the protein content of the plant, an adequate amount of the plant extract was acquired, and Bradford assay was performed. Determine the total protein concentration, in µg/mL, of the acquired plant extract. A bovine serum albumin (BSA) stock solution with a concentration of 250 µg/mL was used and mixtures with the following compositions and absorbance readings were prepared: Volume of BSA (mL) Volume of water (mL) Absorbance Tube # at 595 nm 1 0.00 2.00 0.000 2 0.20 1.80 0.112 3 0.40 1.60 0.225 4 0.60 1.40 0.318 5 0.80 1.20 0.432 6 1.00 1.00 0.551 The absorbance reading of the plant extract is 0.275.
Enzyme chymotrypsin (enzyme digest) Samples: - 1 & 5- Standard Protein (Ladder) - 2 & 6- UNCUT (tube #1) - 3 & 7- 5 mins (tube #2) - 4 & 8- 30 mins (tube #3) Human and Bovine (Left) Chicken and Pigeon (Right) In this experiment we will be comparing the structural similarity of serum albumin from several different vertebrate species and thus examining how closely related the proteins from these species are to each other. These proteins have similar molecular weights. We will first cut the proteins with the enzyme chymotrypsin (enzyme digest). We will then separate the fragments based on their relative sizes through gel electrophoresis so that we can compare the fragments generated by the enzyme digest for the different species. Write the hypothesis and prediction for the experiment.
A student conducted an experiment on protein isolation from mungbean. After isolating the protein, the student characterized the isolate using the Bradford assay. Standard solutions of bovine serum albumin (BSA) were prepared and 0.1 ml of each solution was subjected to Bradford assay. Absorbance readings were made at 595 nm and summarized below. Concentration of Absorbance at BSA (mg/mL) 595 nm 1.2 1.12 1.0 0.97 0.8 0.79 0.6 0.59 0.4 0.37 0.2 0.17 The student found out that 0.1 mL sample of the protein extract from mungbean gave an absorbance of 0.83 in the same assay. 1. How much was the concentration of the protein in the mungbean sample (in mg/mL)? Show all equations and calculations. 2. Draw a graph for the readings of the standard solutions and absorbances. Indicate the approximate location of the calculated concentration of the mungbean sample in your graph.
Suppose you were instructed to repeat this experiment, again using equine albumin antiserum in two tubes. You layer equine serum (containing equine albumin) over the antiserum in one tube and pig serum (containing pig albumin) over the antiserum in the other tube. After incubation, you see precipitous rings in both tubes. Explain these results. Is this due to poor specificity or sensitivity of the test?
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.)
How is 10^4 derived? Please show all calculation steps. # of cells per mL = (Average)*DF*10^4
Dr. Riggs took 1ml of whole mouse blood and added it to 10ml of PBS. You next take 0.5 mL of Dr. Riggs's sample from step 1 and add it to 9.5 mL of PBS. You load your hemacytometer with the dilution you made in step 2, look at it under the microscope, but there are still too many cells to count. You now take 0.2mL of sample from step 2 and add it to 5ml of PBS. Using a hemacytometer, you load your sample and count the following number of red blood cells in 1 chamber (5 squares): chamber 1 = 25, 25, 30, 20, 30 If this mouse has 2 mL of blood in it’s body, how many red blood cells does it have? The options are 1.49X10^6 2.97X10^6 not enough information to tell 1.49X10^9 2.97X10^9
You will be given 1 mL of a 2.0 mg/mL solution of bovine serum albumin (BSA) and 1 mL of a 2.0 mg/mL solution of bovine gamma globulin (BGG). From these solutions, you will need to make 100 μL of each of the following standards using 1x MBP purification buffer as the diluent for preparation of a standard curve: 1000 μg/mL, 750 μg/mL, 500 μg/mL, 250 μg/mL, 125 μg/mL, and 0 μg/mL.
You need to prepare medium for your culture cells. Your salt solution is supplied at a 10X concentration but needs to be 2X for use. You also need to add fetal bovine serum for a final concentration of 8%. What would you add of each for the correct final concentrations in 5 L of media?
I asked earlier a question, and I got this answer. Now, my question is: how do you get the 2.5cm= 100um? I have taken a picture of the paramecium in question, with the scale bar (100um), and a ruler showing it’s measurement is around 2.5cm. Is that how we got the 2.5?
Which fractions measured from your gel filtration experiment had the most and least amount of protein detected? Which fraction likely contained the most myoglobin based off molecular weight and protein presence? Which fraction likely contained the most egg albumin based off molecular weight and protein presence? Which samples measured from your ion exchange experiment had the most protein detected? Calculate the approximate pI of your proteins using the ion exchange Table 2. Ion Exchange Samples Tested by Bradford Assay Concentration BSA (μg/mL) Concentration BSA (mg/mL) Volume of Sample added to Bradford Reagent (μL) Absorbance at 595 nm Standard 1 250 0.25 50 0.32 Standard 2 125 0.125 50 0.16 Standard 3 62.5 0.0625 50 0.08 Standard 4 31.25 0.03125 50 0.04 Standard 5 15.625 0.015625 50 0.02 Blank 0.00 0.00 0.00 Table 3. Gel Filtration Fractions Tested by Bradford Assay Fraction #:…
You will use a Calf Thymus DNA standard stock solution (1 mg/ml) to prepare a standard curve. Calculate volume of stock solution in ul, needed to prepare 10 ug/ml dilution (final volume 1.0 ml).