Equilibration Lab Report

Buckinghamshire, UK) were used within each supplied tube. Each bead contains the desired ingredients needed for the successful PCR reaction, stabilizers, bovine serum albumin to increase overall yield, four deoxynucleotides triphosphates (dNPT), adenine, guanine, cytosine, tyramine ATP, approximately 2.5 units of puReTaq DNA polymerase and a reaction buffer. When reconstituted to the final volume of 22µl, the final volume of each dNTP is 176µM in 8.8mM of Tris-HCL which at room temperature has a pH of 9.0. Finally, 44mM of potassium chloride and 0.66mM of magnesium chloride. All PCR was preformed within a fume cupboard (Bassaire 06HB) to minimise the risk of either moisture or genomic

The procedure for this lab was to punch 30 uniform leaf disks in several spinach leaves, label three plastic cups with: Light, Ambient Light, and Dark. Then prepare a 0.2% solution of sodium bicarbonate and water in a larger beaker and add 2 drops of liquid soap to the solution. Remove the plunger from the syringe and place 10 leaf disk into the syringe. Insert the tip of the syringe into the solution and draw 15-20mL into the syringe. Then seal the tip of the syringe using your index finger and the leaf disk should began to sink.

For Standard Solution 2, we added 3 mL stock solution with 7 mL DI water

The materials used in this lab were distilled water, a vase with Control solution, tap water in a plastic tray. Ag+ solutions with specific concentrations such as, 0.25 (Mm), 0.50 (Mm), 1.00 (Mm), 2.00(Mm), 4.00 (Mm), and AOA solutions with specific concentrations such as, 0.2 (Mm), 0.4 (Mm), 0.6 (Mm), 0.8 (Mm), and 1.0 (Mm), eleven carnations for each group and a razor blade and an electronic balance.

g Kim Chem 127 Ian Shaw November 30, 2015 Equilibrium Lab Objective: The goal of the equilibrium lab is to discover the equilibrium constant for the reaction SCN- and Fe3+. In addition, this lab introduced the concepts of Le Chatelier’s principle and reintroduced Beer’s Law. In addition, this experiment used the spectrophotometry to measure the equilibrium concentrations of FeSCN2+.

Two separate polyacrylamide gels were run at 100V for 60 mins. The gels were transferred to a nitrocellulose membrane and treated with primary and secondary antibodies (Methods2.6.). This was followed with three 5 minute washes with PBS-T, and scanned. The results can be seen in figure 7 as

The first part of the experiment was to isolate the human genomic DNA from cheek cells. The cheek swabbed and cut off the end and inserted it into a microfuge tube. 500 μL of PBS was added to the tube. Then, the tube was shacked and the swab removed then centrifuged for 1 minute at 8,000 RPM. After it was centrifuged, a supernatant was formed with was removed. 300 μL of ACL solution was added to the pellet as well as 20 μL of protease stock solution. This was incubated at 50 ˚C and the temperature rose up to 80˚ C for 10 minutes and centrifuge the tube 30 seconds to remove drops from the lid. The tube was left to cool down then proceeded to be centrifuged and vortexed. Then, 250 μL of supernatant was pipetted into a spin column and an addition

The clarified supernatant was directly purified using a Ni-NTA Spin Column according to instructions supplied by the manufacturer (QIAGEN). Briefly, after washing the column with wash buffer1 (50 mM NaH2PO4 pH 7.5), the supernatant was loaded onto the column, and the column was washed with wash buffer 2 (50 mM NaH2PO4 pH 7.5, 500 mM NaCl, 0.025 Triton X-100 and 20 mM imidazole). The integrase protein was eluted from the column using elution buffer (50 mM NaH2PO4 pH 7.5, 500 mM NaCl, 0.025 Triton X-100 and 400 mM imidazole). The eluted fraction was dialyzed against PBS, and the purity of the integrase protein was assessed by 15% SDS-PAGE and Western Blot. The protein concentration was measured by the Bradford assay, and the purified IntI protein was frozen with 10% glycerol and stored at -20°C until use.

After centrifugation, the volume of each CFE was measured, and then per every mL, .39 grams of ammonium sulfate was weighed out. The CFE was then placed in a beaker that was suspended on top of ice in a larger beaker, which was placed on top of a stir plate. Over a course of 20 minutes, ammonium sulfate was added to the CFE while stirring slowly. After the completing adding all of the ammonium sulfate, solution was stirred for an addition 15 minutes. Followed by centrifugation at 15000 RPM for 20 minutes.

Before adding resin sample was taken out for assay. After bound sample was taken out in separate tube for assay. About 37 mL of the wash buffer was used to wash the undesired proteins. First two and the last two washes were saved for the activity. About 4 mL of the elution buffer was used for eluting the desired protein. All fractions were

The samples were kept in plastic tubes with a closed lid until we were ready for analysis. One gram of the soil was measured out from the tube and mixed with 20ml of deionized water. A serial dilution was prepared consisting of five glass test tubes filled with 9ml of culture broth. Afterwards, 1ml of the soil was piped from the center of the sample and placed into the first tube of the serial dilution. We lightly capped each tube and incubated the sample under a ventilation hood at room temperature (~24ºC) for 48 hours. After the incubation period the samples were mixed well will a vortex. We then piped 1ml of the first dilution into the second dilution and mixed thoroughly with the vortex. This process was repeated with remainder of the dilutions.. Streak plates were prepared in petri dishes filled with premade nutrient agar and 100µl of the third, fourth and fifth dilutions. We streaked an additional

In a tube for each leaf (river plant and dry plant) solution, the following were added; 9 drops of Pi buffer, 6 drops ADP, 6 drops PMS and 6 drop of the plant’s chloroplast solution. The same was done with two tubes containing spinach. ATP was however added to one tube and PMS was not added to the other. Each tube was gently mixed and exposed to light for 10 minutes.

Following the purification process, the enzyme activity assay should reveal luminescence in the supernatant fraction of the tail sample. SDS-PAGE of the samples should reveal a band at 61 kD in the tail sample and no distinct banding in the head sample.

From each centrifuge tube 1ml was placed into separate test tubes, and then 1ml of CuSO4 and Sodium Hydroxide (NaOH) – which gives copper hydroxide (Cu(OH)2), if the colour changed to blue/violet then proteins where present within the solution.

Substituting the value of variables in Table 3 to Equation (7), characteristic roots were obtained: