Category:Team Knights

Figure 3, showing that MglA had ATPase activity. MglA is specifically stimulated by galactose, while being uneffected by other compounds. Indication that the ATPase supports the implication of hydrolysis in protein-dependent transport system. Also figure 2 shows the peak of ATPase activity eluted from column that coincides with the peak of MglA protein.

Figure 3b uses labeled D-proline (with C14) in the presence of Proline reductase and Proline racemase. The 23kDa subunit of the proline reductase became extremely radioactive when placed onto a gel. This indicates that Proline was bound to this peptide.

A clonned KatE gene, inserted in a fermenting bacteria L. lactis was able to produce a catalase and survive in aerobic conditions. Refer to Figure 1. L. Lactis produces an active catalase KatE, and were mixed with H2O2 solution. Catalase activity was detected by bubble formation due to O2 liberation.

As seen in table 2, when the lacG gene was disrupted, the bacteria Streptococcus mutans was unable to grow on TV media containing either galactose or lactose. Also, as seen in table 1, when the lacG gene was disrupted, there was a large reduction of the induction of the lacA promoter by lactose.

Fig. 2 shows a short loop 3, corresponding to LaMP His413–Glu415 in the (α/α)6-barrel catalytic domain of GH65 disaccharide phosphorylase, is identified to be a key determinant for specificity both in phosphorolysis and in regiospecific reverse phosphorolysis. Lactobacillus acidophilus NCFM maltose phosphorylase (LaMP) of the (α/α)6-barrel glycoside hydrolase family 65 (GH65) catalyses both phosphorolysis of maltose and formation of maltose by reverse phosphorolysis with β-glucose 1-phosphate and glucose as donor and acceptor, respectively.

When compared to the doubling time of the wild type strain UA159 of Streptococcus mutans, the growth of JAM2, a galK deficient strain of Streptococcus mutans, had impaired growth equivalent to an organism grown in TV base medium with no added sugar. A measurement of the organism's optical density was used to measure growth. See table 2 for reference.

Figure 5A. shows results of an Era Binding Assay. Era binds to subfractions of the membrane. This is also evidence of Era's presence in the membrane.

Figure 8A. shows that soluble forms of Era, when coupled with GTP, yield both GTP and GDP. This is evidence of GTPase activity.

Using immunocytochemistry and confocal analysis, figure 2 shows that VacA is localized to vacuoles, but not to mitochondria.

Fig. 6 shows that the introduction of the frameshift mutation causes premature termination of the lacR protein product resulting in a loss of repressor activity.

Figure 2b and C FtsZ labeled with GDP for flourences, shows formation of ring during intermediate and late stages of division.

Figure 2b indicates evidence of hydrolase activity, more specificly beta- galactosidase activity.

Figure 4 (A-F) shows flow cytometric analysis using antibodies specific for active Bax to compare cells that were treated with VacA to cells that were not. Bax was activated when exposed to VacA.

Figure 2ab utilizes toxin end point titre and cytotoxic effects on Vero and HT29 cells, while figure 2cd measures toxin neutralization assays. Figure 3a measures the time between innoculation and colonization in the hamster specimins between the different mutants. Figure 3b measures the time from colonization to death of the specimins between the different mutant strains.

Figure 3 shows contrasting glycosylation activity of TcdA and TcdB for various GTPase's (RhoA, Rac1, Cdc42, Rap2A)

Fig.1 showing relative adherence of mutants with mutations in the bgaA gene protein product, indication that the protein is found on cell surface, due to its involvement in cell to cell binding.