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17593303[PMID] - PMC - NCBI

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Items: 5

1.
Figure 4

Figure 4. From: Interaction of Salivary alpha-Amylase and Amylase-Binding-Protein A (AbpA) of Streptococcus gordonii with Glucosyltransferase of S. gordonii and Streptococcus mutans.

Binding of rAbpA and amylase with GtfB. For coating antigens onto wells of ELISA plate, 4, 2, 1, 0.5, and 0.25 μg of either amylase or rAbpA were used. To each well, 1 μg of ligand protein (Gtf-B) was added.

Biswendu Chaudhuri, et al. BMC Microbiol. 2007;7:60-60.
2.
Figure 5

Figure 5. From: Interaction of Salivary alpha-Amylase and Amylase-Binding-Protein A (AbpA) of Streptococcus gordonii with Glucosyltransferase of S. gordonii and Streptococcus mutans.

Growth and biofilm formation of wild-type, abp A and Δgtf mutants of S. gordonii. Bacteria were grown in BM or BM with 1% sucrose and/or 25% saliva. Growth and biofilm formation were measured under CO2 enriched condition. All assays were performed eight times, and mean values and standard deviations are shown..

Biswendu Chaudhuri, et al. BMC Microbiol. 2007;7:60-60.
3.
Figure 3

Figure 3. From: Interaction of Salivary alpha-Amylase and Amylase-Binding-Protein A (AbpA) of Streptococcus gordonii with Glucosyltransferase of S. gordonii and Streptococcus mutans.

Measurement of sucrase and transferase activities of GtfB. Purified GtfB enzyme was incubated at 37°C overnight with sucrose in presence or absence of amylase and/or rAbpA. The amount of glucose and fructose present in the reaction mixtures were measured using the F-kit. Panel A and B. Sucrase activity and transferase activity of GtfB in the presence of amylase and/or rAbpA, respectively. For statistical analysis, Gtf-B activities in the presence of amylase and/or rAbpA were compared with Gtf-B alone.

Biswendu Chaudhuri, et al. BMC Microbiol. 2007;7:60-60.
4.
Figure 2

Figure 2. From: Interaction of Salivary alpha-Amylase and Amylase-Binding-Protein A (AbpA) of Streptococcus gordonii with Glucosyltransferase of S. gordonii and Streptococcus mutans.

Gtf enzyme activity assay. Overnight culture supernatant of strains in question, containing 3 μg total protein were used to precipitate Gtfs. To it, amylase and/or rAbpA was added to a final concentration of 50 μg/ml each. After 2 h at room temperature, precipitates were collected by centrifugation and resuspended in sample buffer and Gtf activity evaluated on SDS-polyacrylamide gel. Panel A. Lanes: 1, 2, and 3, supernatant from abpA- strain (ST); lanes 4,5, and 6, supernatant from Gtf-deficient strain. Panel B. Lanes 1, 2, and 3, supernatant from S. mutans. Panel C. SDS-PAGE gel of precipitates from supernatants stained with SYPRO red. Lanes 1, 2, and 3, supernatants from AbpA-deficient strains; lanes 4, 5, and 6, supernatants from gtf-negative strains of S. gordonii; lanes 7, 8, and 9, supernatants from S. mutans.

Biswendu Chaudhuri, et al. BMC Microbiol. 2007;7:60-60.
5.
Figure 1

Figure 1. From: Interaction of Salivary alpha-Amylase and Amylase-Binding-Protein A (AbpA) of Streptococcus gordonii with Glucosyltransferase of S. gordonii and Streptococcus mutans.

SDS-PAGE analysis of amylase precipitates. Panel A. Precipitates from 18 h culture supernatants, were boiled in sample buffer. The samples containing 3.5 μg of protein were run on 12% SDS-PAGE, followed by staining with SYPRO red in 7.5% acetic acid solution. Lane 1, supernatant of wild type cells (WT); lane 2, supernatant of AbpA-deficient strain (ST); lane 3, supernatant of AbpB-deficient strain (SE); lane 4, molecular mass standard in kDa (M). Panel B. Precipitates from supernatants containing 1.4 μg of protein were used for Gtf-G activity assay. Samples were run on a 12% gel and stained for GTF activity. Lane 1, supernatant from wild type culture (WT); lane 2, supernatant from AbpA-deficient cells (ST); lane 3, supernatant from AbpB-deficient cells (SE). Panel C. Precipitates from supernatants containing 1.4 mg of total protein were used for Western Blot using polyclonal anti-AbpA antibody. Lane1, 2, and 3, supernatants from wild type (WT), AbpA-deficient (ST), and AbpB-deficient cells (SE), respectively.

Biswendu Chaudhuri, et al. BMC Microbiol. 2007;7:60-60.

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