Category:Team Gene Simmons 2013

Table 5 shows that the higher the NSE levels the greater the bad neurological outcome that was observed in patients, this was on day 0 of the study group. In addition, table 6 shows that that there was an increase in neurological worsening for patients in the study group who were administered 25.1-35ng/ml of NSE as shown in the "Yes" category. Futhermore in Figure 1, it shows that the levels of NSE between the controls and study group, in which the study group had a higher level of NSE and thus as shown in the previous tables had more severe neurological function.

Figure 1a shows that the pilO knockout mutant is incapable of producing glycosylated pillin, whereas the wild-type strain did produce glycosylated pillin. Figure 1a shows the picture of the gel from western-blot analysis of whole cell extracts from both the wild-type strain and the pilO mutatnt containing unglycosylated and glycosylated pillin.

Table 2 shows the data for the enzymatic activities of alfB in the presence of various natural fucosylated substrates. The enzymatic activity was determined by measuring the amount of fucose produced(umol) per milligram of enzyme per minute. The data shows that Alfb only causes the catalysis of the hydrolysis of (1->3) linkages between alpha-L-fucose and N-acetylglucosamine residues in glycoproteins.

Figure 3 shows that heterologous expression of SCO1102 in E. coli resulted in increased amounts of fatty acid as well as diacylglycerol compared to the amounts of each produced by the control strain.

Table 2 shows the data for the enzymatic activities of alfA in the presence of various natural fucosylated substrates. The enzymatic activity was determined by measuring the amount of fucose produced(umol) per milligram of enzyme per minute. The data shows that AlfA only catalyzes the hydrolysis of 6'-Fucosyl-GlcNAc.

Figure 5 shows that in an adhesion assay the splA knockout mutant had as little as 5.36% of the adhesion capacity to larval midgut cells compared to that of the ERICII (04-309wt) wild-type allele.

Figure 6 shows that Rv2956 is responsible for catalyzing the O-methylation of position 2 of the terminal fucosyl residue of the phenolic glycolipid produced by M. tuberculosis H37Rv. Figure 6 shows the results of the biochemical analyses of the glycolipid products of the Rv2956 mutant strain.

Figure 1 shows the l-methionine-gamma-lyase knockout mutant fails to produce methanthiol, alpha-ketobutyrate, and ammonia. Figure 1 also shows the wild type strain produces large amounts of methanthiol, alpha-ketobutyrate.

Figure 5 shows that Rv2955c is responsible for catalyzing the o-methylation of position 4 of the fucosyl residue of the phenolic glycolipid produced by M. tuberculosis H37Rv. Figure 5 shows the results of the biochemical analyses of the glycolipid products generated in the two Rv2955c mutant strains.

Figure 4 shows that Rv2954c is responsible for the o-methylation of the hydroxyl group at position 3 of the terminal fucosyl residue of the phenolic glycolipids produced by M. tuberculosis. This conclusion is supported by the differences observed in the biochemical analyses of the glycolipid product of the Rv2954c mutant (PMM115:pPET1)compared to the same analyses of the glycolipid product of the wild-type strain. The biochemical analyses presented in figure 4 include: MALDI-TOF Mass Spec, 1D 1H-NMR, and 2D-COSY.