The experiment conducted was to determine the expression of the lac z gene under different treatment conditions. The first treatment was to add 0.3% glucose to the E. coli. The second was to add 0.2% lactose. The third treatment was similar to the second one, in which 0.2% lactose was added, except at a later time. The only difference between these trials is the time the lactose was added. Treatment four was adding 0.3% glucose and 0.2% lactose to the E. coli. After the data was gathered, the treatments were analyzed through absorbance and the time required for reactions to take place.
Table 1 summarizes the information about the bacterial growth, such as the OD600 reading shows how bacteria grew in each sample during the incubation period. As the figure indicates, the samples that contained glucose had a higher OD600 reading, which indicates that the bacteria samples grew much better in glucose rich environments compared to the environments containing lactose. Also, the samples that have higher Abs420 readings for less reaction time indicate that there is a higher presence of active β-galactosidase which can interact with the ONGP. The information in Figure 1, which was obtained through a β-galactosidase activity assay, indicates that the samples with lactose and no glucose have the higher activity level for β-galactosidase, where the samples that did not have the lactose added later were able to have a higher reaction rate with the ONGP.
The amounts of β-galactosidase present in the four samples is confirmed by the results of a Western blot, shown in Figure 2, which indicates that there is a higher level of the protein in those samples, and it also indicates that there is little to no β-galactosidase produced within th...
... middle of paper ...
...ny qualities that make it an easy protein to detect (2009). This could also be used in many other transgenic experiments by using it as a selectable marker, where only the cells that have it could survive in lactose, or by viewing it as a gene that loses its ability to function after the gene insertion where the lack of β-galactosidase would indicate that the gene of interest was correctly inserted.
Forss-Petter S, Danielson PE, Catsicas S, Battenberg E, Price J, Nerenberg M, Sutcliffe JG. 1990. Transgenic mice expressing beta-galactosidase in mature neurons under neuron-specific enolase promoter control. Neuron 5(2): 187-97
Debacq-Chainiaux F, Erusalimsky J, Campisi J, Toussaint O. 2009. Protocols to detect senescene-associated beta-galactosidase (SA-β gal) activity, a biomarker of senescent cells in culture and in vivo. Nature Protocols 4: 1798-1806
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