Among these methods, the hydrothermal method is used to prepare ZnO nanorods due to its low cost and simplicity [16, 25, 26]. In order to improve the structural and optical properties of Cu-doped ZnO nanorods, the effect of the Cu precursor is worth clarification. In the study reported here, we have synthesized pure and Cu-doped ZnO nanorods onto a quartz substrate this website pre-coated with a ZnO seed layer using the hydrothermal method. The main focus has been put on the effect of the copper precursor on the morphology, structural, transmittance,

and photoluminescence properties of the synthesized ZnO nanorods. Methods The nanorod growth was accomplished in two steps: (1) the sputtering of ZnO seed layer to achieve highly aligned Cu-doped Fer-1 nmr ZnO nanorods [27] and (2) the nanorod growth using the hydrothermal method. Sputtering of ZnO seed layer Prior to the nanorod growth, a 120-nm-thick seed layer of undoped ZnO was deposited onto a quartz substrate using RF magnetron sputtering at room temperature. Before the deposition of the ZnO seed layer, a surface treatment of the quartz substrate was conducted using acetone, ethanol, and deionized water for 10 min for each at RT and then dried in

air. Pure ZnO (99.999%) with a 50-mm diameter and 5-mm thickness was used as the ZnO target. The seed layer sputtering was accomplished in a mixture of O and Ar gas atmosphere with the gases’ flow rates of 2.5 and 35 sccm, respectively. The base

pressure attained was 10−4 Pa, and the working pressure was 1 Pa during sputtering. The sputtering power was 100 W. In order to remove the contaminants TPCA-1 from the ZnO target, pre-sputtering for 10 min was performed. Finally, the ZnO-sputtered seed layer thin films were annealed at 500°C for 30 min. Nanorod growth Undoped and Cu-doped ZnO nanorods were grown by the hydrothermal method on a quartz substrate seeded with the ZnO thin film using hexamethylenetetramine (HMT) ((CH2)6 N4), zinc acetate dihydrate (Zn(CH3COO)2 · 2H2O), Edoxaban and either cupric acetate (Cu(CH3COO)2 · H2O) or cupric nitrate (Cu(NO3)2 · 3H2O) as hydroxide, zinc (Zn), and copper (Cu) precursors, respectively. The nanorod growth was accomplished by suspending the substrates in a conical flask containing the aqueous solution that was prepared from zinc acetate (0.025 M) and HMT (0.025 M). Before suspending the samples, the aqueous solution was magnetically stirred for 30 min. The flask that contains the equimolar aqueous solution was placed in a combusting waterbath deposition system at 90°C for 90 min. After the nanorods were grown, the samples were removed from the beakers, rinsed in deionized water several times to remove the unreacted materials, and then finally dried in an oven at 60°C for 2 h. In order to introduce the Cu dopants, either cupric acetate (0.025 M) or cupric nitrate (0.

And no attempt has been reported so far in analysis of the ECPs of A. pleuropneumonae. The complete genome sequence of A. pleuropneumonia JL03 provided an essential database for applying immunoproteomic approach to JL03. In the present study, we report this approach to JL03 for the first time which involved the identification of immunogenic buy Thiazovivin proteins from its OMPs and ECPs. Results and Discussion 2-DE profile of the ECPs and OMPs, immunoblotting analysis and identification of immunogenic proteins In

the present study, linear immobilized pH gradient strips (3–10 L IPG 13 cm) and 10% SDS-PAGE gels were used for the prepared samples separation. Figure 1A and 1B show the 2-DE profile of OMPs and ECPs of A. pleuropneumoniae JL03. The 2-DE and immunoblotting RG7112 cost were repeated three times and the results were reproducible. A total of 110 spots and 98 spots were detected on the silver-stained gels of OMPs and ECPs respectively by the software ImageMaster v 6.01. After immunoblotting analysis with convalescent sera, 28 immunoreactive spots from OMPs (Figure 1A and 1C) were identified, and they represented 17 proteins. Chung et al. recently

identified 47 OM proteins from A. pleuropneumoniae 5b with an optimized extraction protocol based on the sucrose-density gradient which yielded preparations highly enriched for OM proteins and lipoproteins[8], and 10 of the 47 OM proteins were identified as immunogenic proteins in this study. In addition, Rhonda et al. recently demonstrated the sucrose-density selleck chemicals llc gradient extraction of outer membranes in Campylobacter jejuni produced purer sample than

carbonate extraction [9] that was applied in this study. So further study needs to be tried on immunoproteomic analysis of other serotypes of A. pleuropneumoniae with the optimized OMP extraction protocol of Chung et al. for search of more immunogenic OMPs. All the 19 immunoreactive spots from ECPs (Figure 1B and 1D) that represented 16 proteins were identified whereas no specific immunoreactive protein spot was observed from OMPs and ECPs using control sera. The detailed Peptide Mass Fingerprinting Methane monooxygenase (PMF) results of the immunoreactive proteins are listed in supplemental table S1 [see additional file 1]. Overall, values of gel estimated pI and MW are matched well with their theoretical ones but some discrepancies still exist. Similar migration for several proteins has been observed in proteomic analysis of other pathogens previously[10, 11]. This might be due to the presence of natural isoforms, posttranslational processing, and/or modification, or an artifact caused by sample preparation. Figure 1 2-DE profile of ECPs and OMPs and immunoblot. 2-DE profile of OMPs (A) and ECPs (B) from A. pleuropneumoniae JL03 strain. Preparative gel stained with Silver Nitrate. Immunoblot of OMPs and ECPs from convalescent sera (C) and (D).

pastoris GS115 pPICZαA-32cβ-gal methanol induced variant (B) and P. pastoris GS115 pGAPZαA-32cβ-gal constitutive variant (C). Lanes 1 – protein weight marker. Panel A: lane 2 – cell selleck inhibitor extract after expression, lane

3 – purified β-D-galactosidase after affinity chromatography. Panel B and C: lane 2 – broth after protein expression, lane 3 – protein precipitate, lane 4 – purified β-D-galactosidase after affinity chromatography. In the P. pastoris expression system the methanol induced and constitutive biosynthesis variants for larger scale production of the enzyme were tested. By cloning the gene in the form of translational fusion with the S. cerevisiae α-factor leader sequence under the control of either the methanol induced promoter AOX1 or under the constitutive promoter GAP, pPICZαA-32cβ-gal and pGAPZαA-32cβ-gal recombinant expression plasmids were constructed. P. pastoris GS115 strain was transformed with linearized pPICZαA-32cβ-gal or pGAPZαA-32cβ-gal plasmids. The obtained P. pastoris GS115 recombinant strains harbouring pGAPZαA-32cβ-gal or pPICZαA-32cβ-gal recombinant plasmids were used for extracellular production of the Arthrobacter sp. 32c β-D-galactosidase (Fig. 2B, lane 2 and Fig. 2C, lane 2). The applied overexpression systems were efficient, C188-9 cost giving see more approximately 137 and 97 mg (Table 1) of purified β-D-galactosidase (Fig. 2B and 2C, lanes 4) from 1 L of induced culture for the AOX1 and constitutive system, respectively. Noteworthy

is the fact that all attempts in extracellular expression of β-D-galactosidase from Pseudoalteromonas sp.22b [10, 11] previously described by us did not succeed (data not shown). pheromone The corresponded β-D-galactosidase is a tetramer composed of 115 kDa subunits. All the amount

of produced protein with fused secretion signal was accumulated in the cells. We also tried to produce the Pseudoalteromonas sp. 22b β-D-galactosidase in the form of fusion protein with other secretion sequences: PHO5 and STA2. All attempts gave negative results. It seems that molecular mass of desired recombinant protein is limited for extracellular production by P. pastoris host. Characterization of Arthrobacter sp. 32c β-D-galactosidase The temperature profiles of the hydrolytic activity of the recombinant Arthrobacter sp. 32c β-D-galactosidase showed that the highest specific activity with ONPG was at 50°C (155 U/mg). Lowering or raising temperature from 50°C resulted in the reduction of β-D-galactosidaseactivity. Recombinant β-D-galactosidase exhibited 15% of the maximum activity even at 0°C and approximately 60% at 25°C (Fig. 3). In order to determine the optimum pH for recombinant β-D-galactosidase, we measured the enzyme activity at various pH values (pH 4.5–9.5) at 0–70°C, using ONPG as a substrate. β-D-galactosidase exhibited maximum activity in pH 6.5 and over 90% of its maximum activity in the pH range of 6.5–8.5 (Fig. 3). Figure 3 Effect of temperature on activity of recombinant Arthrobacter sp.

J Occup Rehabil 19:231–237.

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