ResultsThe experiment conducted consisted of determining the expression of the lac z gene in different treatment conditions. The first treatment consisted of adding 0.3% glucose to E. coli. The second was to add 0.2% lactose. The third treatment was similar to the second, in which 0.2% lactose was added, except at a later time. The only difference between these studies is when the lactose was added. Treatment four involved adding 0.3% glucose and 0.2% lactose to the E. coli. After collecting data, treatments were analyzed through absorbance and the time required for reactions to occur. Table 1 summarizes the bacterial growth information, for example the OD600 reading shows how the bacteria grew in each sample during the incubation period. As the figure indicates, samples that contained glucose had a higher OD600 reading, indicating that bacteria samples grew much better in glucose-rich environments than in lactose-containing environments. Additionally, samples exhibiting higher Abs420 readings for a shorter reaction time indicate that there is a greater presence of active β-galactosidase that may interact with ONGP. The information in Figure 1, obtained through a β-galactosidase activity assay, indicates that samples with lactose and no glucose have the highest activity level for β-galactosidase, whereas samples without lactose added they were subsequently able to have a higher reaction rate with ONGP. The amount 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 protein in those samples, and also indicates that there is little or no β-galactosidase produced in the paper medium, 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 cells possessing it could survive in lactose, or by considering it as a gene that loses its ability to function after gene insertion where the lack of β -galactosidase would indicate that the gene of interest has been inserted correctly. Works Cited 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 the control of the neuron-specific enolase promoter. Neuron 5(2): 187-97Debacq-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's protocols 4: 1798-1806