Study on the influence of a magnetorheological finishing path on the mid-frequency errors of optical element surfaces.

Magnetorheological finishing (MRF) is a deterministic optical processing technique based on CCOS that achieves high removal efficiency and processing accuracy while reducing subsurface damage. This technique still suffers from multiple iterations of processing due to variations in removal efficiency and the inability to fully correct mid-frequency errors below the cut-off frequency of the removal function. For the above problems, this paper attempted to establish the error model of removal function efficiency change for predicting the change of MRF efficiency. Based on the analysis of the distribution of surface shape residuals under different machining paths, a process combining spiral scanning and raster scanning is proposed, which can realize the correction of surface shape and restrain the deterioration of mid-frequency errors. The experimental results show that when the low-frequency errors of fused silica element surface converge rapidly, by optimizing the machining removal coefficient and using the spiral scanning and raster scanning combined method, the PSD analysis results show that the mid-frequency errors of the combined process is lower than the initial value, which expands the process route for the MRF of high-precision optical elements.

Responses of sedimentary δ2Halk values to environmental changes as revealed by different plant responses to altitude and altitude-related temperatures.

Single species-based altitudinal transects may provide a new understanding of the variabilities in sedimentary wax-derived n-alkane hydrogen isotope (δ2Halk) values caused by altitude and complex climatic change linked with the growth of mountains. We investigated Kobresia pygmaea (Kobresia), Quercus aquifolioides (Quercus) and Berberis thunbergii DC (Berberis) along three altitudinal transects on the Tibetan Plateau (TP), i.e., the southern TP, the Longmen Mountains (LM; eastern TP) and the Qilian Mountains (QL; northeastern TP). Here we present 47 plant δ2Halk values: these include 14 Kobresia, 27 Berberis and 6 Quercus samples, which are accompanied by comparisons with nine new soil δ2Halk values from the QL, and 105 previously-published δ2Halk values for surface soils along the first two transects. Our data show that altitude is the dominant factor in determining three plant δ2Halk values. However, we observed substantial differences in the δ2Halk values and their εwax-p ratios for Kobresia, Quercus and Berberis for different climatic regimes and along these three transects. Significantly, for Kobresia along the LM and QL transects, ∆δ2Halk = -84.3‰/km (r2 = 0.94; p < 0.05; n = 4) and - 65.5‰/km (r2 = 0.74; p < 0.01; n = 10), and ∆εwax-p = -80.4‰/km (r2 = 0.93; p < 0.05) and -56.7‰/km (r2 = 0.66; p < 0.01), respectively, were three or four times as large as for the soil δ2Halk values observed along these altitudinal gradients. Overall, the altitudinal lapse rate (ALR) of δ2Halk values and their εwax-p ratios varies between species, with Kobresia being the most negative and Berberis the least negative, potentially resulting from the strong response of monocotyledoneae Kobresia δ2Halk values to cooling with increasing altitude, and the relative influence of cryosphere meltwater at higher altitudes. Thus, impact of climate change on the sedimentary δ2Halk values should therefore be fully taken into account during reconstructions of paleoaltitudes.

Adenylate Cyclase AcyA Regulates Development, Aflatoxin Biosynthesis and Fungal Virulence in Aspergillus flavus.

Aspergillus flavus is one of the most important opportunistic pathogens of crops and animals. The carcinogenic mycotoxin, aflatoxins produced by this pathogen cause a health problem to human and animals. Since cyclic AMP signaling controls a range of physiological processes, like fungal development and infection when responding to extracellular stimuli in fungal pathogens, in this study, we investigated the function of adenylate cyclase, a core component of cAMP signaling, in aflatoxins biosynthesis and virulence on plant seeds in A. flavus. A gene replacement strategy was used to generate the deletion mutant of acyA that encodes the adenylate cyclase. Severe defects in fungal growth, sporulation and sclerotia formation were observed in the acyA deletion mutant. The defect in radical growth could be partially rescued by exogenous cAMP analog. The acyA mutant was also significantly reduced in aflatoxins production and virulence. Similar to the former studies in other fungi, The acyA mutant showed enhancing tolerance to oxidative stress, but more sensitive to heat stress. Overall, the pleiotropic defects of the acyA deletion mutant indicates that the cAMP-PKA pathway is involved in fungal development, aflatoxins biosynthesis and plant seed invasion in A. flavus.

Fabrication of a totally renewable off-channel amperometric platform for microchip electrophoresis.

In this approach, a novel method to fabricate an integrated amperometric platform used in off-channel electrophoresis has been introduced. A simple screen printed protocol combining a wet etching procedure was used to define the pattern on a glass substrate, and whole electrodes were constructed by filling the conductive carbon ink into the etched cavities. A simple Teflon tape was used to align this platform with the micro-channel, and the variation of reassembling of this device can be down to 2.2% without the assistance of microscope. This device was characterized by dopamine (DA) and catechol (CA), and the width of half peak is around 4s, even a 100 µm double T shape injection design and a 550 µm working electrode were used in this work. Under the optimum condition, this device possesses a low background with a noise level of 1.4 pA (peak to peak). The linear range for DA and CA are 0.1-100 µM (R = 0.998) and 0.2-200 µM (R = 0.996) with a theoretical plate number of 1.57 × 10(4) and 3.46 × 10(4) (plate/m), respectively.

Low-potential amperometric determination of purine derivatives through surface oxide regeneration method.

This article described a novel amperometry which can be used for determination of purine derivatives including uric acid, xanthine, hypoxanthine, guanine, and adenine without surface contamination. By applying a constant potential of -0.125 V (vs. Ag/AgCl) in a flow injection system, the chelating capability of these purine derivatives converts the cuprous oxide layer into a soluble complex. This behavior would dissolve the passive oxide layer and expose the bottom copper layer to the solution, subsequently; an oxidation current which attributed to the regeneration of the original cuprous oxide layer is used to reflect the concentration of these purine derivatives. In a 50mM phosphate buffer, pH 7.0, this approach provides a high sensitivity with LOQ of sub-micro molar level of five purines and high stability with a RSD of 2.5% for 10 µM xanthine (N=12). This method does not suffer from most biological species including ascorbic acid, acetaminophen, creatine, dopamine, sarcosine, ammonium ion, chloride ion, and urea at equal or higher than its physiological concentration.

Amperometric determination of NADH with Co3O4 nanosheet modified electrode.

In this work, we have developed a simple and reliable cobalt oxide (Co3O4) based amperometric sensor for the determination of NADH. A sheet shape Co3O4 nanooxide was synthesized by the CTAB assisted hydrothermal technique and was characterized by SEM and XPS. Owing to the redox property of Co3O4, the operating potential of NADH can be significantly reduced from 0.7 down to 0.1 V. Compared to a commercial Co3O4 nanoparticle modified electrode, this nanosheet form cobalt oxide possesses a rapid background subsiding characteristic and a low residual current. This scheme was conducted on a flow injection system with a constant operating potential of 0.1 V (vs. Ag/AgCl, 3 M) in a 0.2 M phosphate buffer at pH 6.0. A suitable linear range from 10 to 100 µM (R=0.999) with a detection limit of 4.25 µM (S/N=3) was obtained. The RSD for 20 successive measurements of 75 µM NADH is only 1.4%, which indicates a high stability and no contamination during NADH oxidation. This scheme did not suffer from conventional antioxidants, including dopamine, uric acid, epinephrine, serotonin, histamine, and 4-acetaminophen, except ascorbic acid. Thus, an ascorbate oxidase was introduced to remove the ascorbic acid before the sample was injected into the flow injection analysis system. After this simple pretreatment, the influence of ascorbic acid was eliminated, successfully.

A novel structural specific creatinine sensing scheme for the determination of the urine creatinine.

In this work, a highly structural dependent amperometric scheme was proposed for the determination of creatinine without enzymatic assistance. The principle of this novel method is based upon the formation of a soluble copper-creatinine complex on the copper electrode surface. Subsequently, an oxidative current from the regeneration of the surface oxide layer is monitored and it is proportional to the concentration of the creatinine. This scheme can be conducted at potential of -0.1 V (vs. Ag/AgCl, 3 M) in phosphate buffer (pH 7). A typical calibration plot from 25 µg/dL to 1.5 mg/dL (R(2)=0.997) with a detection limit of 6.8 µg/dL (S/N=3) is achieved. The relative standard deviation of 21 successive injections of 0.2 mg/dL creatinine is 0.018. Under the optimal conditions, the frequently encountered biological interferences at physiological or higher concentration were investigated. Only uric acid revealed an obvious interference (298.1%). However, a Nafion(®) coated copper plating electrode shows a successful decrement of the interference of the uric acid with slightly decreased sensitivity of creatinine. The feasibility of this scheme for further clinical application is demonstrated by both HPLC and FIA to evaluate the creatinine concentration in a urine sample.

Affinity chromatography of DNA on nonporous copolymerized particles of styrene and glycidyl methacrylate with immobilized polynucleotide.

Nonporous particles of microsize were prepared by the dispersion polymerization of styrene and glycidyl methacrylate and chemically modified to introduce amino groups on the surface by grafting with either hexamethylenediamine or N-methyl-1,3-propanediamine. Aminated particles were then coupled with phosphorylated single-stranded polynucleotides at the 5'-end through covalent linkages. The affinity columns packed with these prepared polynucleotide-immobilized particles effectively retained single-stranded DNA, which could base-pair with the immobilized sequence. Bound DNAs could be eluted to yield a sharp peak by using an aqueous solution of 0.4M NaOH. The nonspecific adsorption due to the electrostatic interaction between the polynucleotide and the residual amino groups on the particle surface via the amination with hexamethylenediamine was significant and could only be reduced by using a high salt (NaCl) concentration. A higher salt concentration in the elution solution could result in a portion of complementary polynucleotide eluted in the nonretained fraction. However, the nonspecific adsorption of polynucleotides was insignificant in the column packed with DNA-immobilized particles prepared via amination using N-methyl-1,3-propanediamine. The column was effective for microanalysis of sequence-specific DNA.

Influence of Surface Hydrophobic Groups on the Adsorption of Proteins onto Nonporous Polymeric Particles with Immobilized Metal Ions.

Iminodiacetic acid (IDA) and octyl moieties were covalently bound on nonporous particles, which were prepared from dispersion polymerization of methyl methacrylate and glycidyl methacrylate. After being charged with copper ions, the IDA-bound particles could specifically adsorb deoxyribonuclease I (DNase I) through the affinity interaction between protein and immobilized metal ion. A mixed-ligand (metal-chelate and octyl-bound) support was obtained after hydrophobic (octyl) groups were also introduced to the particle surface. The affinity adsorption of DNase I on the copper-IDA chelate was influenced by interaction between the protein and the bound octyl group. Both the affinity and the hydrophobic interactions could be well described by the Langmuir isotherms. The equilibrium adsorption constants were estimated separately to be 0.96 and 0.50 liter g(-1) for affinity and hydrophobic bindings, respectively. For binding on mixed-ligand support, the adsorption constant was 0.45 liter g(-1). It was evident that both affinity and hydrophobic interactions are involved in the adsorption of proteins onto mixed-ligand particles. Desorption of the inactive proteins from the support was possible by increasing the hydrophobicity of the solution. Copyright 2001 Academic Press.