For part 2 of the experiment (please refer to next page for Figure 3), Figure 3 shows a graph comparing the absorbance readings of the Glutamate-pyruvate aminotransferase serum with the time in minutes. A similar rate was predicted to occur for both the assays done. This would be characterized by the readings showing two parallel lines on the graph. However, the two first readings did not demonstrate this. This could possibly be due to different and insufficient amounts of NADH+ being added to the serums, which would mean that the reaction would not occur as fast as normal and at different rates. A third assay was carried out, which was not parallel to either of the previous assays, but most likely to be accurate as the correct amount of NADH+ was added. The third absorbance reading did however, show two outliers at the end of the line that did not follow the trend.
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Thus, calculations (in appendix) were carried out separately for all three assays. More care should be taken when carrying out such an experiment.
Misreading of the quantities of products was what led to the inaccuracies in the results.
The rate of the reaction (the rate at which NADH/H+ is oxidized and the use of the lactose dehydrogenase) was proportionate to the specific activity of the serum glutamate-pyruvate aminotransferase. As glutamate pyruvate produced pyruvate, it reacted with NADH/H+ to form lactate and NAD+ at the same rate. Assay 3 had the fastest rate of reaction, and so had the largest value for its specific activity, at 0.01019 micromoles per milligram per minute. This supports the idea that the previous two assays had an insufficient amount of NADH+ added, which would hinder the reaction producing lactate and NAD+. Assay 1 and assay 2 had much slower reaction rates, at
7.9149 × 10 (-4) and 2.8444 × 10(-3) micromoles per milligram per minute respectively.
All other substances were the same, and added in the same quantities, so should not have affected the
Thus, calculations (in appendix) were carried out separately for all three assays. More care should be taken when carrying out such an experiment.
Misreading of the quantities of products was what led to the inaccuracies in the results.
The rate of the reaction (the rate at which NADH/H+ is oxidized and the use of the lactose dehydrogenase) was proportionate to the specific activity of the serum glutamate-pyruvate aminotransferase. As glutamate pyruvate produced pyruvate, it reacted with NADH/H+ to form lactate and NAD+ at the same rate. Assay 3 had the fastest rate of reaction, and so had the largest value for its specific activity, at 0.01019 micromoles per milligram per minute. This supports the idea that the previous two assays had an insufficient amount of NADH+ added, which would hinder the reaction producing lactate and NAD+. Assay 1 and assay 2 had much slower reaction rates, at
7.9149 × 10 (-4) and 2.8444 × 10(-3) micromoles per milligram per minute respectively.
All other substances were the same, and added in the same quantities, so should not have affected the