determine the activity of G6Pase Essay

The dependent variable in the experiment was the temperature and energy absorbed by the water.

    One possible source of error that can affect the results was that a mercury thermometer was used instead of an electronic one. The use of a mercury

Controls- The control in this experiment was very important because if it was not contained, then the data would have been faulty. It was very difficult to keep

This lab is performed in order to determine the total energy in a reaction between zinc and hydrochloric acid. The reaction is done twice, once to measure the heat of the reaction and again to determine the work done in the system. This is because Enthalpy equals heat plus work (∆H= ∆E+W). Heat and work can be broken down further into separate components so the equation used in lab is ∆H=mc∆T + PV. Many calculations are used in the lab to find out what cannot be measured directly (ex: volume). After all the calculations were complete it was shown to have a very small percent error.

After the substrate solution was added, five drops of the enzyme were quickly placed in tubes 3, 4 and 5. There were no drops of enzyme added in tubes 1 and 2 and in tube 6 ten drops were added. Once the enzyme solution has been added the tubes were then left to incubate for ten minutes and after five drops of DNSA solution were added to tubes 1 to 6. The tubes were then placed in a hot block at 80-90oC for five minutes. They were then taken out after the five minute period and using a 5 ml pipette, 5 ml of distilled water were added to the 6 tubes and mixed by inversion. Once everything was complete the 6 tubes were then taken to the Milton Roy Company Spectronic 21 and the absorbance of each tube was tested.

The experiment is repeated twice and an average is obtained. This ensures the consistency of the measurement as the reading is triplicated, thus reducing anomalies. It can be seen that the reading obtained were around the same value. This proves that the results are reliable.

One of our flaws was that the temperature of the water was not exactly the same when we did the different trials. The temperatures were slightly off from our recorded value during the experiments. The change in temperature would affect the time it took for the Alka-Seltzer tablet to dissolve in the water. If there was a direct relationship between water temperature and dissolve time, we would not be able to see it because the temperatures are off and the dissolve times are not associated with the correct temperature. Another flaw is that we did not use the same amount of water throughout the experiment. We used a beaker to measure the water, which did not result in accurate measurements. The difference in amount of water could result in a difference in reaction time. The third flaw in the experiment was that during the reaction of the warm water, the water in the cup overflowed and spilled, bringing some of the Alka-Seltzer tablet with it. There were different amounts of tablet in different areas of the water, which means a different amount of Alka-Seltzer remained inside of the cup in each trial. This difference would mean that data for the warm water would fluctuate and we would not have accurate

From the stock substrate solution of 2.5 mM, each group serially diluted at least one different substrate concentration for a total of four different substrate concentrations to be investigated: 1.25 mM, 1.0 mM, 0.75 mM, 0.25 mM. The enzyme concentration was kept constant at 2.0 mM while experimenting on the affect of varying enzyme concentration on the rate and product formation of ONP. Enough 2.0 mM enzyme solution was prepared in the previous part of the project to supply this assay. Using similar procedure to collect absorbance data as the first part, 0.5 mL of 2.0 mM enzyme concentration was placed into the cuvette and used to calibrate the spectrometer at 420 nm. Data was then started, with the immediate addition of 0.5 mL of varying substrate concentrations. Each varying substrate concentration was split between the team and run for a total of 10 minutes, with the exception of the 1.25 mM run. Upon completion, data from each varying substrate concentration was copied to a single Excel sheet and used to produce an absorbance vs. time graph, product formation vs. time graph, Michaelis Menten plot, and Lineweaver-Birk plot. This analysis was used to calculate the V0,Vmax, and Km for β-Galactosidase

Assays are used as an indicator of whether or not the purification process is working correctly, or if the proteins have been destroyed in the process (1). The lab consisted of purifying wheat germ by utilizing the enzyme that is already present in the substance itself, acid phosphatase. Acid phosphatase was being separated from the wheat germ using a centrifuge (a machine that spins at high speeds in order to separate substances with different densities in a solution) during each step of the experiment to continuously separate and purify the sample (3). There were three assays in which were used during the experiment. One assay used during the experiment was a Bradford dye reagent, which was a blue dye that was added to samples of the supernatant to display the different concentrations of proteins present in each. Another assay that was used during the lab was the KOH. This reagent was added to different samples of the supernatants than what were used for the Bradford dye. The KOH was used to help stop the reaction that had originally taken place from the addition of the acid phosphatase reagent in step three, but its main use was to distinct the different concentrations of the proteins present in each step of the purification

However the lab being investigated used the relative concentration of catalase as the independent variable and the oxygen produced in 10min as the dependant variable. However it was noticed that the amount of oxygen conceived by the experimenters with different catalase concentrations had quantitative values very similar to those of the data in question. The lab also proved how the greater concentration in catalase increased the amount of oxygen liberated, evidently the lab in question also had an increase in oxygen liberated however with a greater quantity of hydrogen peroxide. Furthermore it is important to notice the mean data for the lab in question is 42.86 cm^3, although the mean data for lab being investigated is 55cm^3, relative to the time and independent variable, the data remains quite similar. Likewise the lab in question was compared to that of a second lab, THE DECOMPOSITION OF HYDROGEN PEROXIDE BY LIVER CATALASE. By" JOHN WILLIAMS. The lab being investigated shared the exact same catalase solution for the lab thus making it more accurate to the lab in question. Similarly the following lab effectively proved that the greater amount catalase solution in the experiment, the greater velocity the decomposing will have. The results are quite different than the lab in question due to the fact that the IV and DV are both changed in the following lab. Although the results increase, the labs ultimately prove two separate things that are very much linked

G6PD is one of many enzymes that help the body process carbohydrates and turn them into energy. G6PD also protects red blood cells from potentially

These results suggest that a major source or sources of error occurred during the lab. Until additional runs of this lab are carried out the source of error remains ambiguous. However, while we cannot specifically point out the source of error, clearly major sources of error could include poor sample preparation, issues related to the spectrophotometer, or possibly inadequate enzyme samples due to age or contamination.

BglA was remain active even in the existence of 600 mM glucose. However, BglA activity was gradually repressed with the increase of glucose concentration, and Ki value for glucose was found to be 1200 mM as shown in figure 4b. Organic solvents have proven an obvious constrain for the BglA activity, enzyme was completely inactive by adding 40% (v/v) methanol, ethanol, n-butanol and isopropanol whereas, 40% (v/v) acetone, ethyl acetate and acetonitrile strongly repressed BglA activity up to 18%, 38%, 50%, respectively.

The substrates of glycerate kinase are ATP and D-glycerate and the products are ADP and 3-phospho-D-glycerate. This enzyme belongs to the family of transferases.1 Other common names include: glycerate kinase (phosphorylating), D-glycerate 3-kinase, D-glycerate kinase, glycerate-3-kinase, GK, D-glyceric acid kinase, and ATP: D-glycerate 2-phosphotransferase. 1 This enzyme participates in 3 metabolic pathways: serine/glycine/threonine metabolism, glycerolipid metabolism, and glyoxylate-dicarboxylate metabolism.1

To find the effect of temperature on the activity of an enzyme, the experiment deals with the steps as follows. First, 3 mL if pH 7 phosphate buffer was used to fill three different test tubes that were labeled 10, 24, and 50. These three test tubes were set in three different temperature settings. The first test tube was placed in an ice-water bath for ten minutes until it reached a temperature of 2° C or less. The second tube’s temperature setting was at room temperature until a temperature of 21°C was reached. The third tube was placed in a beaker of warm-water until the contents of the beaker reached a temperature setting of 60° C. There were four more test tubes that were included in the procedure. Two of the test tubes contained potato juice were one was put in ice and the other was placed in warm-water. The other two test tubes contained catechol. One test tube was put in ice and the other in warm water. After