Bovine Serum Albumin Protein Lab Report

The cuvette was placed in the spectrophotometer with the arrows, on both the cuvette and the SpectroVis, facing the same side. After the recording, the cuvette was removed from the SpectroVis and the content was poured back into the original volumetric flask. The absorbance as well as the maximum wavelength of each solution was recorded in Table 3 and

Although the overall absorbance increases as more milliliters of mitochondrial suspension is added to a mixture of 0.25 mL of 0.5 mM DCIP, 0.5 mL of 50 mM sodium azide, various volumes of assay buffer (20 mM potassium

Each sample of solution #3 being tested by the three reagents will have the most noticeable change in color in result of a positive reaction between solution #3 and the reagent. 5. We took three samples of three solutions, a positive control, and a negative control (fifteen test tubes total.) Each sample was tested by Benedict’s, Biuret’s, and Lugol’s Reagent for a reaction. The result of the reaction was then recorded in notes.

You could use Beer’s Law to calculate the unknown concentration of cobalt (II) nitrate as Beer’s Law states that a solutions concentration is proportional to the solutions concentration. Based on this, if you had the equation for Beer’s Law you could then plug in the unknown solutions absorbancy at 750 nm to find the

Record the amount of absorbance by converting transmittance every 5 minutes for a total of 20 minutes. Repeat all of these steps for the cantaloupe, banana, replacing the blank each time to recalibrate the spectrophotometer. After recording all the percent transmittance value, the data was then converted into absorbance value by using the absorbance conversion table. The information was placed on a plotted graph

Abstract This laboratory experiment investigated how different types of media plates affect the growth of skin microflora mainly microflora in the nostril It was hypothesized that the nostril microflora were gram-positive bacteria that belong to the genera Streptococcus, Staphylococcus and Propionibacteria. Results showed that the nostril microfloras were gram-positive (stained purple). However, gram staining was not enough to prove that the bacterium obtained from the nostril are Streptococcus, Staphylococcus, and Propionibacteria spp. The results do not fully support the hypothesis.

SOD activity was calculated in terms of units/mg protein. Total protein thiols (TPT) - This assay is based on the principle of formation of relatively stable yellow color by sulphydryl groups with DTNB (Moron et al., 1979). Briefly, 0.2 ml of liver homogenate was mixed with phosphate buffer (pH 8.0), 40 µl of 10 mM DTNB and 3.16 ml of methanol. This mixture was incubated for 10 min and the absorbance was measured at 412 nm against appropriate blanks.

Starch solution is then placed into the test tube at a quantity of 5 mL. 5 drops of Lugol’s Iodine solution is added to the test tube. If the color changes, then it is known that starches are present in the solution. Proteins are next tested. In order to do this, 5 mL of gelatin solution is added to the test tube. 10 drops of Biuret’s reagent are added to test for protein.

The pigment is produced due to quorum sensing of bacteria, when an appropriate level of N-hex anoyl-L-homoserine lactone (HHL),

In a non-reducing sugar 3cm cubed and 10 drops of hydrochloric acid is placed in a test tube for a water bath of 5 minutes to be mixing afterwards. Biurets reagent is added to the protein solution to determine it presence. Testing for

Using the samples in the cuvettes, calculate the absorbance by inserting them into the spectrophotometer. Record these results and use them to calculate the concentration of the drug left in the blood, by using the calibration curve. To construct a calibration curve, make up solutions of Eosin and water in seven separate tubes using table 1 and calculate the absorbance of each. Plot the calibration curve with this absorbance vs. the final

The precipitate was dialyzed and used for enzyme purification using column chromatography. The dialyzed sample was loaded on DEAE-cellulose column, which was equilibrated previously with the buffer A (50 mM sodium phosphate buffer, pH 7.4). The column was washed with the five bed volumes of buffer A, and the enzyme was eluted with buffer A

Amino acids are organic compounds that are the building blocks for proteins (Bruice). They are composed of a carboxylic acid with a protonated amino group and a hydrogen on the alpha carbon (Bruice). Amino acids have various side chains that provide proteins with great structural diversity, and in turn, functional diversity (Bruice). Amino acids can be divided into polar, non-polar, acidic, and basic (Bruice). The amino acids used in this experiment are Phenylalanine, Leucine, Lysine, and Alanine.

The 3 concentrations of enzymes were 0.5 ml, 1.0 ml, and 2.0 ml of turnip extract, while the substrate consisted of 0.1ml, 0.2 ml, and 0.4 ml of hydrogen peroxide. In a separate tube, the control was made up of turnip extract and guaiacol, known as the color reagent. This was recorded the absorbance every 20 seconds for 3 minutes.

Coomassie G-250 is doubly protonated in acidic conditions and appears red in color; however, when bound to the basic amino acids of the protein, the dye shifts to the anionic blue form. As the protein and dye interact, an electron is donated to the charged groups within the protein so that the protein structure is disrupted and the hydrophobic pockets are exposed. The sulfonic groups of the dye bind to the amines within the exposed hydrophobic pockets to shift the dye to the anionic blue form. This color change is measured spectroscopically and is a direct correlation to the concentration of protein.10 Consequently, the BSA standard is used for comparison, because the basic and aromatic amino acid compositions are similar between the BSA standard and alkaline