Advantages And Disadvantages Of Protein

Perform a series of accurate tests on biological molecules to detect the presence of carbohydrates and proteins, as well as the action of an enzyme on specific molecules.

The weight obtained was recorded as initial weight. While weighing the dialysis tube with the solution of starch and sodium sulfate, eight test tubes were obtained and solution of starch/sodium sulfate was added to two test tubes labeled bag start (Keith et al., 2010).

This Lab Report is an analysis of the results of a two-part experiment. In the first part, we used a gel filtration column to separate the components of a mixture composed of protein and non-protein molecules. By doing so we hoped to obtain fractions that contained single components of the mixture, while also gaining insight into the relative molecular weight of each component compared to each other. We would then plot these fractions onto nitrocellulose paper in order to determine which fractions had protein. In the second part, we would use the fractions which we had determined had protein to conduct an SDS-PAGE. By doing so we hoped to determine an estimate on the molecular weight of the proteins present in each fraction by comparing it to a tracker dye composed of a variety of molecules of differing molecular weight.

Colorimetric assay is a process of determining a concentration of a solution based on absorbance of light. The purpose of this lab is to determine if the Bradford assay is an accurate way to determine an unknown concentration of two samples of protein. The Bradford assay is done by measuring wavelength of light passing through a cuvette filled with Bradford dye and concentrations of PBS and proteins. After the cuvettes are mixed they are placed into a spectrophotometer to measure wavelength. The wavelength given will be used to plot a standard curve based on concentration (x-axis) and wavelength (y-axis). The standard curve is then used to measure an educated guess on the concentrations of unknown protein concentrations. We hypothesized that if we use the Bradford assay and colorimetric spectrophotometry we can determine an accurate concentration of two unknown concentrations of proteins. The results of this lab failed to reject our hypothesis based on accurate measurements of protein concentrations. The standard curves are drawn with a linear increasing slope. The Bradford assay is an accurate way to demine the concentration of an unknown concentration.

Salting out is the first isolation technique carried out for this lab. This isolation technique separates the Rubisco based on solubility. The method of salting out requires an addition of salt such as ammonium sulfate to the solution containing protein Rubisco to allow precipitation (Duong-Ly & Gabelli, 2014). The additional of ammonium sulfate to the Rubisco

Figure 1 contains gel electrophoresis for protein samples. The lanes were labeled from 1 to 10 from the right to the left. Lane 1 contained the ladder fragment. Lane 2 contained the filtrate. Lane 3 contained the S1 sample. Lane 4 contained the P1 sample. Lane 5 contained the P1 medium salt sample. Lane 6 contained the P1 high salt sample. Lane 7 contained the S2 sample. Lane 8 contained the P2 sample. Lane 9 contained the P2 medium salt sample. Lane 10 contained the P2 high salt sample.

d. You don’t know the molecular weight (MW) of protein X and you are not able to find that information in the scientific literature. The best way to determine the MW of a protein using an SDS-PAGE gel is to use the protein ladder bands to create a Log(MW) vs. Rf graph and calculate the MW from the line of best fit. What is the equation to calculate the Rf of a protein band? Make a table of the Log(MW) and the Rf values for all 5 protein ladder bands. Describe any trends you see in the table

Gel electrophoresis method. Qualitative analysis shows protein concentrations in kidney, heart, and liver. 1-6 are kidney tissue. 7-14 are liver and 15-19 are the heart tissue.

After cooled down a little, mix with a glass stirring rod until sample is uniform in texture and appearance, then re-weigh the sample.

vials are dry on the inside. Place a small wad of absorbent cotton in the bottom of each vial and, using a dropper, add 10 drops of 15% KOH per respirometer. Do not get KOH on the sides of the respirometer. Place a small wad of dry nonabsorbent cotton on top of the KOH-soaked absorbent

Load the remaining protein mix into the column, and this will begin to bind within the column. Once the solution has settled, fill the column with NaCl a total of four times; as the wash is flowing through, collect and label the protein solution in fractions, and save for the

The food was prepared at the room temperature of 21.1°C. The sides of the vial were wiped with a paper towel to remove any excess food. The netting was folded to fit inside the vial and then the vial was closed using a cotton plug. (USF,

3. The tubes are allowed to incubate in a 37˚C water bath for 1 hour. The final pH of the solutions is tested and the amount of protein digestion is estimated using a scale of (+++), (++), (+), and (-) by

2. Allow the beaker to cool until it reaches room temperature; then weigh the beaker with the contained solid. The loss in mass represents the amount of NH4Cl in your

As a result, the interactions between protein molecules exceed protein-water interactions, and the solubility decreases. Moreover, the differences in the amino acid sequence makes proteins differ in their salting in and salting out behavior. This is the basis for the fractional precipitation of proteins by means of salt. Most commonly used salt is ammonium sulfate because it is available in highly purified form and because of its high solubility. (Boyer, 2000)