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Mehta PK, Kalra M,

Anal Biochem 2012, 431:4.CrossRef 19.

Mehta PK, Kalra M, Khuller GK, Behera D, Verma I: Development of an ultrasensitive polymerase chain reaction-amplified immunoassay based on mycobacterial RD antigens: implications for the serodiagnosis of tuberculosis. Diagn Microbiol Infect Dis 2012, 72:166.CrossRef 20. Niemeyer CM, Adler M, Wacker R: Immuno-PCR: high sensitivity Quisinostat solubility dmso detection of proteins by nucleic acid amplification. Trends Biotechnol 2005, 23:208.CrossRef 21. Notomi T, Okayama H, Masubuchi H, Yonekawa T, Watanabe K, Amino N, Hase T: Loop-mediated isothermal amplification of DNA. Nucleic Acids Res 2000, 28:E63.CrossRef 22. Fu S, Qu G, Guo S, Ma L, Zhang N, Zhang S, Gao S, Shen Z: Applications of loop-mediated isothermal DNA amplification. Appl Biochem Biotechnol 2011, 163:845.CrossRef 23. Mori Y, Nagamine K, Tomita N, Notomi T: Detection of loop-mediated isothermal amplification reaction by turbidity derived selleck inhibitor from magnesium pyrophosphate formation. Biochem Biophys Res Commun 2001, 289:150.CrossRef 24. Parida M, Sannarangaiah S, Dash PK, Rao PV, Morita K: Loop mediated isothermal amplification (LAMP): a new generation of innovative gene amplification technique; perspectives in clinical diagnosis of infectious diseases. Rev Med Virol 2008, 18:407.CrossRef

25. Mori Y, Notomi T: Loop-mediated isothermal amplification (LAMP): a rapid, accurate, and cost-effective diagnostic method for infectious diseases. J Infect Chemother 2009, 15:62.CrossRef 26. Kaneko H, Kawana T, Fukushima E, Suzutani T: Tolerance of loop-mediated isothermal amplification to a culture medium and biological substances. J Biochem Biophys Methods 2007, 70:499.CrossRef 27. Nagamine K, Hase T, Notomi T: Accelerated reaction by loop-mediated isothermal amplification using loop primers. Mol Cell Probes 2002, 16:223.CrossRef 28. Goto M, Honda E, Ogura A, Nomoto A, Hanaki K: Colorimetric

detection of loop-mediated isothermal amplification reaction by using hydroxy naphthol blue. Biotechniques 2009, 46:167.CrossRef 29. Schweitzer Amisulpride B, Wiltshire S, Lambert J, O’Malley S, Kukanskis K, Zhu Z, Kingsmore SF, Lizardi PM, Ward DC: Immunoassays with rolling circle DNA amplification: a versatile platform for ultrasensitive antigen detection. Proc Natl Acad Sci USA 2000, 97:10113.CrossRef 30. Schweitzer B, Roberts S, Grimwade B, Shao W, Wang M, Fu Q, Shu Q, Laroche I, Zhou Z, Tchernev VT, Christiansen J, Velleca M, Kingsmore SF: Multiplexed protein profiling on microarrays by rolling-circle amplification. Nat Biotechnol 2002, 20:359.CrossRef 31. Wiltshire S, O’Malley S, Lambert J, Kukanskis K, Edgar D, Kingsmore SF, Schweitzer B: Detection of multiple allergen-specific IgEs on microarrays by immunoassay with rolling circle amplification. Clin Chem 1990, 2000:46. 32.

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These findings further support a role of carbonyl injury in the p

These findings further support a role of carbonyl injury in the pathogenesis and the potential benefits of antioxidant therapy [23]. Taurine (2-aminoethanesulfonic acid) and gamma-aminobutyric acid (GABA) are both natural amino acids with wide occurrence. In the context of the neural system, taurine and GABA are inhibitory amino acid neurotransmitters, and glutamate and aspartate are excitatory amino acids. Taurine was originally described to inhibit lipid peroxidation [24].

At present, taurine has been demonstrated to protect the brain against lipid peroxidation and oxidative stress [25, 26]. It has also been shown that GABA exhibits anti-hypertensive effect, activates the blood flow, and increases the oxygen supply ICG-001 manufacturer in the brain to enhance metabolic function of brain cells [27]. Evidence suggests GABA-improved visual cortical function in senescent monkeys [28]. Decreased proportion of GABA associated with age-related degradation of neuronal function and neuronal degenerative diseases [29]. Recent study showed GABA-alleviated oxidative damage [30]. Glutamate (Glu) and aspartate (Asp) are reported to prevent cardiac

toxicity by alleviating oxidative stress [31]. In this paper, it is hypothesized Tipifarnib mw that several amino acids may inhibit the formation of ALEs and scavenge reactive carbonyl compounds such as MDA based on a potential carbonyl-amine reaction under physiological conditions, and its function is in vitro compared; also, the strong inhibition function of amino acids was investigated in vivo. Methods Materials and preparation Taurine, GABA, Glu, and Asp were purchased from Sinopharm Chemical Reagent C., Ltd (Shanghai, China). 1,1,3,3-Tetramethoxypropane (TMP) and pentylenetetrazol (PTZ) were obtained from Fluka Chemie AG (Buchs, Switzerland). MDA detection kit, superoxide dismutase (SOD) detection kit, glutathione peroxidase (GSH-Px) detection kit, and total below protein quantification

kit (Coomassie Brilliant Blue) were purchased from Nanjing Jiancheng Bioengineering Institute (Nanjing, China). Other chemicals used were purchased from HuiHong Chemical Reagent C., Ltd. (Changsha, China). MDA stock solution (40 mM) was prepared by hydrolyzing TMP according to a method described by Kikugawa and Beppu [32]. Thus, 0.17 mL (1.0 mmol) of TMP was added in 4 mL of 1.0 M HCl and shaken at 40°C for about 2 min. After the TMP was fully hydrolyzed, the pH was adjusted to 7.4 with 6.0 M NaOH, and the stock solution was finally made up to 25 mL with 0.2 M PBS (pH 7.4). The stock solution was checked by measuring the absorbance at 266 nm using ϵ 266 = 31,500 M−1 cm−1. In vitro incubation experiments and HPLC, fluorescence, and LC/MS analysis of the incubation mixture Several amino acids were incubated with MDA (5.0 mM) in 5 mL of 0.2 M PBS at 37°C (pH 7.4).

In the field of probiotic studies, characteristic proteomic profi

In the field of probiotic studies, characteristic proteomic profiles can be identified for individual

properties which may serve as bacterial biomarkers buy Captisol for the preliminary selection of strains with the best probiotic potential. This would certainly increase the chances of success of clinical trials through a more focused approach. Methods Strain characterization and standard culture conditions Lactobacillus strains used in this study were identified at the species level by recA PCR (data not shown) [51]. All cultures were maintained as frozen stocks held at -80°C in Cryobank cryogenic beads (Bio-Rad, Hercules, CA, USA). For experimental use, strains were cultured anaerobically (Anaerocult A system, Merck, Darmstadt, Germany) at 37°C in selleck compound Man-Rogosa-Sharpe broth (Biokar, Beauvais, France) see more supplemented with 0.05% (w/v) L-cysteine hydrochloride monohydrate (MRSC; Merck) to early stationary phase, using three successive subcultures (1% v/v inoculation; 12-15 h). Bile salt tolerance Tolerance to bile was assessed by investigating the ability of strains to grow in the presence of different concentrations of bovine bile (Oxgall,

Sigma-Aldrich, St Louis, MO, USA), as previously described [52]. Fresh cultures were inoculated (0.1%, v/v) into MRSC broth containing 0.5%, 1.0%, 1.8%, and 3.6% (w/v) Oxgall and incubated anaerobically at 37°C. Bacterial growth was monitored in honeycomb plates (Oy Growth Curves AB, Helsinki, Finland) by measuring the optical density at 600 nm (OD600) every 30 min for 48 h using an automated turbidimetric system (Bioscreen C MBR, Oy Growth Curves AB). Three independent experiments were carried out and each assay was performed in triplicate. Comparison of cultures was based on their growth rates in each broth, expressed as a percentage of that of the control which was assigned a value of 100% [52]. Tau-protein kinase Using Statgraphics plus 5.1 software (Manugistics,

Rockville, MD, USA), data were subjected to two-way ANOVA with strain and bile concentration as variables. Multiple comparison test using least significant difference procedure was carried out to compare means for which the ANOVA test indicated significant mean differences (p < 0.05). Whole cell protein extraction The following experiments (including 2-DE) were performed for bacterial cells cultured in two different broths (MRSC and MRSC supplemented with 3.6% Oxgall). Early stationary phase cells from a 10-mL broth culture were harvested and washed three times with phosphate-buffered saline (PBS). Cell pellets were resuspended in 2 mL of PBS and cryobeads of these suspensions were prepared in liquid nitrogen. The bacterial beads were ground in liquid nitrogen using a cryogenic grinder (6870 Freezer/Mill, Spex CertiPrep, Stanmore, UK) with three steps of 3 min at a rate of 24 impacts/s. After sample centrifugation (5000 g for 5 min, 4°C), supernatants were filtered through a 0.45-μm pore size filter (Chromafil PET; Macherey-Nagel, Düren, Germany).

We have previously described

an in vitro system that allo

We have previously described

an in vitro system that allows us to measure mutation and transformation frequencies in H. pylori wild type strains and isogenic gene knock-out mutants, as well as the length of the donor DNA fragments imported into the recipient chromosome after transformation [12]. In this system, natural transformation of different H. pylori wild type strains with DNA from heterologous H. pylori donors led to the incorporation of 1.3-3.8 kb fragments into the recipient chromosome, depending on the combination Selleck Caspase inhibitor of donor and recipient strains. Imports resulting from recombination contained short interspersed sequences of the recipient (ISR) in ~10% of the cases [12, 13], leading to complex mosaic patterns. The glycosylase MutY, a member of the base excision repair (BER) machinery, is involved in at least one ISR-generating pathway in H. pylori, repairing mismatches after the heteroduplex formation between recipient and donor DNA [12]. However, the inactivation of mutY in H. pylori did not Selleck CT99021 completely abrogate the formation of ISR, suggesting that additional mechanisms might contribute to ISR generation. In addition to BER, H. pylori also contains a second gap-filling DNA repair system, the nucleotide excision repair pathway (NER), whose role in H. pylori mutation and PD0332991 recombination is yet poorly understood. In Escherichia coli, the NER

system is responsible for the replacement of bulky DNA lesions such as covalently modified bases, noncovalent drug nucleotide complexes and abasic sites generated by oxidative metabolism or ionizing radiation [14, 15]. Initiation of NER starts with the recognition of DNA distortions by the UvrAB complex [16]. After recognition, UvrA dissociates and UvrC is recruited and acts as a single-stranded DNA endonuclease, cleaving at both sides of the lesion CYTH4 [17, 18]. Finally, the unwinding activity of the UvrD helicase, which preferentially catalyzes a 3’ to

5’ unwinding, removes the excised segment. DNA polymerase I fills in the gap while the remaining nick is closed by ligase [19, 20]. In H. pylori, orthologs of the four NER genes, uvrA-D, have been identified [21]; but until now, only few studies have addressed the functions of these genes. H. pylori UvrB was shown to be involved in the repair of acid-induced DNA damage [22], and UvrD limited homologous recombination and DNA damage-induced genomic rearrangements between DNA repeats [23]. Here we have used a genetic approach to analyze the roles of the H. pylori NER system components in regulating the mutation rate, and the frequency and import patterns of homologous recombination after natural transformation. Results Characterization of H. pylori NER mutants and their susceptibility to UV light-induced cell damage To investigate how the NER system contributes to genetic diversification in H. pylori, we individually inactivated the NER genes in H.

Transference may thus be the main factor explaining the presence

Transference may thus be the main factor explaining the presence of virulence genes in diazotrophic symbionts (e.g., homologous virB1-virB11 in Rhizobium (= Agrobacterium)tumefaciens and Mesorhizobium loti R7A) [20, 21] as well as nitrogen-fixing genes in pathogenic bacteria (e.g. homologous to the cluster fixNOQPGHIS in the pathogens Brucella melitensis and Pseudomonas aeruginosa) [22]. In addition, it has also been demonstrated

that the plant pathogen R. tumefaciens is capable of nodulating legumes after receiving a symbiotic plasmid [23]. However, until now, the functional evidence of the natural coexistence of genes for symbiosis and pathogenicity has been demonstrated only in strains of R. rhizogenes [24]. Despite the intriguing evolutionary questions raised in the analysis of symbiotic and pathogenic bacteria of the this website order Rhizobiales, very few studies of comparative genomics with a significant number of distinct genera and representative species

of both lifestyles have been conducted between species of this prokaryotic order. In this study we have done such see more comparisons aiming at increasing the existent knowledge about the evolutionary divergence of these biological processes. Results Phylogenetic reconstructions were performed in order to analyze the dynamics of the symbiosis and/or pathogenesis processes along the evolution of the species in study. The phylogenetic reconstruction model obtained with the 104 concatenated housekeeping proteins of 25 species and 30 strains with complete genome available presented a branched topology of two Selleck Salubrinal groups – one Tideglusib composed mostly of photosynthetic, methylotrophic, and bioremediation bacteria; and the second composed mostly of symbiotic and pathogenic bacteria. The second group is further subdivided into two major subgroups, one with the symbionts (except for R. tumefaciens, a pathogen showing

high similarity with the symbionts), and another gathering the pathogens (Figure 1). Non-symbiotic nitrogen-fixing bacteria and bacteria involved in bioremediation closer to symbionts and pathogens in study may assist in the origin and ancestry genes and the gene flow occurring in Rhizobiales, and were considered in the comparisons. Figure 1 Phylogeny model reconstructed with 104 housekeeping concatenated proteins of representatives of the Rhizobiales order. Phylogeny model reconstructed with 104 housekeeping concatenated proteins of 30 strains (belonging to 25 species) of the order Rhizobiales. The Neighbor-Joining method was applied with Phylip 3.67 program and 1,000 replicates for bootstrap support. Representatives of the beta-Proteobacteria class were used as the outgroup.

0–1 2 No restriction No restriction Stage 3A (overt nephropathy:

0–1.2 No restriction No restriction Stage 3A (overt nephropathy: early) ≥60 mL/min, overt proteinuria Normal 25–30 0.8–1.0 7–8 No restriction Stage 3B (overt nephropathy, late) <60 mL/min, proteinuria > 1 g/day Mild restriction Avoid overwork 30–35 0.8–1.0 7–8 Mild restriction Stage 4 (renal failure) Azotemia, proteinuria Moderate restriction AZD2014 in vivo 30–35 0.6–0.8 5–7 1.5 Stage 5 (dialysis) – Moderate restriction Hemodialysisb 35–40 1.0–1.2 7–8 <1.5   Avoid overwork CAPDb 30–35 1.1–1.3

8–10 Mild restriction aFor hypertension: less than 6 g/day bHemodialysis (HD) and continuous ambulatory peritoneal dialysis (CAPD) patients are catabolic. Total calorie intake should be slightly increased compared to DM patients. In CAPD patients, glucose is absorbed from PD fluid. References are the reports to MWL 1992, 1993 and Japan DM Association, 1999 Table 19-2 (b) Lifestyle modification for DM Foretinib price nephropathy (2) Stage Exercisea Work House work Pregnancy · Delivery Treatment, Diet, Daily life Stage 1 (pre-nephropathy) • Basically do exercise for DM • Normal • Normal OK • Control blood glucose, Avoid excessive PF-6463922 in vivo protein intake Stage 2 (early nephropathy) • Basically do exercise for DM • Normal • Normal OK • Strict control of blood glucose • Anti-hypertensive treatment • Avoid excessive protein intake Stage

3A (overt nephropathy: early) • Basically exercise is OK • Amount of exercise is dependent of the condition • Stop excess exercise • Normal • Normal Not allowed • Strict control of blood glucose • Anti-hypertensive

treatment • Protein restrictionb Stage 3B (overt nephropathy: late) • Restrict exercise • Slight exercise to maintain physical strength • Restrict exercise • Normal~slight restriction, depend on the job • Mild restriction • Work up to feel fatigue Not allowed • Control of blood glucose • Anti-hypertensive treatment, protein restrictionb • Water intake should be determined with Metformin price the degree of edema and congestive heart failure Stage 4 (renal failure) • Restrict exercise • Walking or warm-up exercise is OK • Slight restriction ~restrict job • Avoid fatigue • Stop over-work, No night shift • Restricted • Not overwork: feel no fatigue Not allowed • Control of blood glucose and hypertension • Low protein dietb (until dialysis) • Water intake should be determined with the degree of edema and congestive heart failure Stage 5 (Dialysis) • Basically slight exercise only • Stop excess exercise • Basically, mile restricted work • Avoid overwork, Restrict extra-work • Normal • Not overwork: feel no fatigue Not allowed • Control of blood glucose and hypertension • Dialysis or renal transplantation • Restrict water intake (inter-dialytic weight gain: less than 5% of ideal weight) aDegree of restriction is dependent on proteinuria or hypertension.

Paris D, Beaulieu-Abdelahad D, Bachmeier C, Reed J, Ait-Ghezala G

Paris D, Beaulieu-Abdelahad D, Bachmeier C, Reed J, Ait-Ghezala G, Bishop A, Chao J, Mathura V, Crawford F, Mullan M: Anatabine

lowers Alzheimer’s Abeta production in vitro and in vivo. Eur J Pharmacol 2011, 670:384–391.PubMedCrossRef 12. Paris D, Beaulieu-Abdelahad D, Abdullah L, Bachmeier C, Ait-Ghezala G, Reed J, Verma M, Crawford F, Mullan M: Anti-inflammatory activity of anatabine via inhibition of STAT3 phosphorylation. Eur J Pharmacol 2013, 698:145–153.PubMedCrossRef 13. Beck TW, Housh TJ, Johnson GO, selleck screening library Schmidt RJ, Housh DJ, Coburn JW, Malek MH, Mielke M: Effects of a protease supplement on eccentric exercise-induced markers of delayed-onset muscle soreness and muscle damage. J Strength Cond Res 2007, 21:661–667.PubMed 14. Haass M, Kubler learn more W: Nicotine and sympathetic neurotransmission. Cardiovasc Drugs Ther 1997, 10:657–665.PubMedCrossRef

15. Connolly DA, Reed BV, McHugh MP: The repeated bout effect: Does evidence for a CHIR98014 cell line crossover effect exist? J Sports Sci Med 2002, 1:80–86. 16. Nosaka K, Clarkson PM: Muscle damage following repeated bouts of high force eccentric exercise. Med Sci Sports Exerc 1995, 27:1263–1269.PubMedCrossRef 17. McHugh MP, Tetro DT: Changes in the relationship between joint angle and torque production associated with the repeated bout effect. J Sports Sci 2003, 21:927–932.PubMedCrossRef 18. Housh TJ, Cramer JT, Weir JP, Beck TW, Johnson GO: Physical Fitness Laboratories on a Budget. Scottsdale, AZ: Holcomb Hathaway Publishers; 2009. 19. Beck TW, Kasishke PR 2nd, Stock MS, Defreitas JM: Eccentric exercise does not affect common drive in the biceps brachii. Muscle Nerve check details 2012, 46:759–766.PubMedCrossRef 20. Cockburn E, Robson-Ansley P, Hayes PR, Stevenson E: Effect of volume of milk consumed on the attenuation of exercise-induced muscle damage. Eur J Appl Physiol 2012, 112:3187–3194.PubMedCrossRef 21. Rawson ES, Gunn B, Clarkson PM: The effects of creatine supplementation on exercise-induced muscle damage. J Strength Cond Res 2001, 15:178–184.PubMed 22. vanGreevenbroek MM, Schalkwijk CG, Stehouwer CD: Obesity-associated low-grade inflammation in type 2 diabetes mellitus: causes and consequences. Neth J Med 2013, 71:174–187. 23.

Masternak MM, Bartke A: Growth hormone, inflammation and aging. Pathobiol Aging Age Relat Dis 2012, 2:17293. 24. Osorio FG, Barcena C, Soria-Valles C, Ramsay AJ, de Carlos F, Cobo J, Fueyo A, Freije JM, Lopez-Otin C: Nuclear lamina defects cause ATM-dependent NF-kappaB activation and link accelerated aging to a systemic inflammatory response. Genes Dev 2012, 26:2311–2324.PubMedCrossRef 25. Connolly DA, Sayers SP, McHugh MP: Treatment and prevention of delayed onset muscle soreness. J Strength Cond Res 2003, 17:197–208.PubMed 26. Omvik P: How smoking affects blood pressure. Blood Press 1996, 5:71–77.PubMedCrossRef 27. Lee IW, Ahn SK, Choi EH, Lee SH: Urticarial reaction following the inhalation of nicotine in tobacco smoke. Br J Dermatol 1998, 138:486–488.PubMedCrossRef 28.

For this purpose, the PP-g-PAA fabric was immersed in 0 1 M NiCl2

For this purpose, the PP-g-PAA fabric was immersed in 0.1 M NiCl2 solution for 12 h. After filtration, washing with distilled water, and drying at ambient temperature, the resulting PP-g-PAA (Ni) fabric was added to 2.5% solution of potassium hexacyanoferrate(II) for 24 h under gentle mixing. Finally, the KNiHCF-loaded PP fabric was separated by filtration, washed with deionized water until clear rinsing solution, and dried at 60°C for 24 h. Characterization of the KNiHCF-loaded polypropylene fabric The surface morphology of the original

PP and KNiHCF-loaded PP fabrics was recorded by a Hitachi S-4100 field emission scanning electron microscope (SEM; Hitachi, Ltd., Tokyo, Japan) at an acceleration

voltage Captisol mw of 15 keV. The elemental composition was performed by energy-dispersive X-ray spectroscopy (EDS). The studied samples were sputter-coated with a thin Pt layer prior to examination. Fourier transform infrared (FT-IR) measurements were carried out using a Spectrum™ 100 FT-IR spectrometer (PerkinElmer, Waltham, MA, USA) with attenuated total reflectance (ATR) mode. Spectra were collected by cumulating 24 scans. X-ray diffraction studies were carried out on a DRON-3 diffractometer (Scientific Industrial Enterprise “Burevestnik”, St. Metalloexopeptidase Petersburg, Russia) using Cu-Kα radiation in the range 10° to 90°

in 2θ at room temperature. Adsorption experiments A cesium Selleckchem Doramapimod chlorite stock solution of 1,000 mg/l was diluted, as required, to obtain the desired concentration. The pH of the solution was adjusted by using dilute solutions of hydrochloric acid, or sodium hydroxide, depending on the requirement. Adsorption experiments were carried out in batch mode under shaking by placing a dry nanocomposite fabric (0.1 g) in a series of polypropylene flasks with 20 ml of CsCl solution. Once the required time elapsed, the residual solution was filtered through a Whatman filter paper and analyzed for Cs KPT-330 clinical trial concentration by the atomic absorption spectrophotometer model AA-8500 (Nippon Jarrell-Ash Co., Ltd., Kyoto, Japan). The amount of Cs adsorbed by the synthesized nanocomposite adsorbent at time t, Q t (mg/g), was calculated as follows: where C 0 and C t are the initial concentration and concentration of Cs at time t (mg/l) in the experimental solution, V is the volume of the solution (l), and W is the weight of the adsorbent (g). At the equilibrium time, Q t  = Q e . Adsorption efficiency α (%) at equilibrium was calculated as follows: where C e is the cesium concentration at equilibrium. All the experiments were performed in duplicate.

coli K-12 on GlcNAc results in the induction of the nag regulon t

Growth of E. coli K-12 on GlcNAc results in the induction of the nag regulon that includes nagBACD in one operon and the divergently transcribed operon with the nagE gene coding for the GlcNAc transport protein, EIINag[3]. However, it has also been reported that in E. coli K92 the GlcNAc transport protein is induced by both GlcNAc and Aga [9]. Although, in our CHIR-99021 mw qRT-PCR assays we only examined nagA and nagB expression and not nagE expression, the expression pattern of nagA and nagB should reflect that of nagE expression because they are all part of the nag regulon

[3]. Therefore, unlike what was observed in E. coli K92 [9], our data (Table 1) show that in EDL933 and E. coli C nagA and nagB were induced only by GlcNAc and not by Aga PI3K inhibitor and thereby it would be reasonable to conclude that nagE was also not induced by growth on Aga. This discrepancy between our observation with two strains of E. coli, EDL933 and C, and that observed in E. coli strain K92 [9] is probably due to strain difference. Table 1 Analysis of gene expression in EDL933, E. coli C, and their mutants by qRT-PCR Carbon Sourcea Strain Relative expression of genes in EDL933 and E. coli C

b     agaA agaS nagA nagB Glycerol EDL933/E. coli C 1/1 1/1 1/1 1/1 Aga EDL933/E. coli C 375/32 495/62 1/1 1/1 GlcNAc EDL933/E. coli C 1/3 1/3 12/16 24/23 Glycerol EDL933 ∆agaA /E. coli C ∆agaA ND/NDc 1/1 1/1 1/1 Aga EDL933 ∆agaA /E. coli C ∆agaA ND/ND 699/86 16/7 28/9 GlcNAc EDL933 ∆agaA /E. coli C ∆agaA ND/ND 5/3 12/9 20/13 Glycerol EDL933∆nagA /E. coli C ∆nagA 2/0.5 Torin 2 chemical structure 2/0.2 ND/ND 61/19 Aga EDL933∆nagA /E. coli C ∆nagA 820/179 917/93 ND/ND 8/2 a Carbon source used for growth. b The relative expression values after the forward slash is that of E. coli C. c ND indicates not detected. In ∆agaA mutants Digestive enzyme of EDL933 and E. coli C, the expression of agaA could not be detected, as expected, irrespective of the carbon source used for growth (Table 1). When these two ∆agaA mutants were grown on glycerol, the expression levels of

agaS, nagA, and nagB were unchanged compared to that of the wild type strains grown on glycerol. When the ∆agaA mutants of EDL933 and E. coli C were grown on Aga, the induction of agaS was about 700-fold and 90-fold, respectively, which is140% higher than that in their parent strains grown on Aga (Table 1). Thus, the relative expression level of agaS was higher in ∆agaA mutants grown on Aga. In Aga grown ∆agaA mutants, nagA and nagB were significantly induced whereas, these genes were not induced at all in wild type strains grown on Aga. In fact, in Aga grown EDL933 ∆agaA, the relative expression levels of nagA and nagB were about 130% compared to that of their expressions in wild type EDL933 and EDL933 ∆agaA grown on GlcNAc.