Sodium periodate

A single hydrogel bead was put into each of five separate individual plastic container (include a cover with screw thread) that containing sodium periodate solution (0.7mole.L -1 ) for variable soaking time (1-5hours) then each of the single hydrogel bead was transferred to the gel bead cell fixed in the manifold reaction system. From the results obtained it was noticed that a maximum response was obtained when using a period of three hours as soaking time for the sodium periodate solution. CONSTRUCTION OF THE CALIBRATION GRAPH

in presence of mercuric acetate as a scavenger. The reaction between sodium periodate and proline in alkaline medium shows 2:1 stoichiometry. The values of rate constants observed at different temperatures (30 to 45 0 C) were utilized to calculate the activation parameters. A mechanism involving the complex formation between catalyst, substrate and oxidant has been proposed. L-glutamic acid has been identified as main oxidation product of the reaction chromatographically and spectroscopically. Based on kinetic data, reaction stiochiometry and product analysis of the reaction a feasible mechanism has been proposed. The rate law has been derived from obtained kinetic data.

In this study, we attempted to identify additional molecules on Vero cells that could have affinity for dengue virus and facilitate virus infection. This paper therefore reports the spe- cific binding of dengue virus to two molecules of 74 and 44 kDa on Vero cells. Binding of the virus to the 74-kDa molecule was susceptible to protease and sodium periodate treatments and resistant to treatment by heparinases. Lectins such as concanavalin A (ConA, which binds to ␣-mannose residues on N-linked high-mannose or hybrid glycans) and wheat germ agglutinin (WGA, which recognizes acetylglucosamine [GlcNAc␤1-4] on N-linked glycans) prevented dengue virus binding to both the 74- and the 44-kDa protein in overlay assays, while phytohemagglutinin-P (PHA-P, which recognizes oligosaccharides) did not affect binding to either of the cellular molecules, suggesting the participation of carbohydrate resi- dues such as ␣-mannose or N-acetylglucosamine in virus bind- ing to host cells. A polyclonal antibody raised against the 74-kDa protein localized the protein on the surfaces of Vero cells in immunofluorescence assays. The antibodies were also able to inhibit dengue virus infection. These data suggest that during dengue virus infection of Vero cells, HS might serve as a primary receptor, probably concentrating virus particles on the cell surface, and that subsequent viral penetration could require other molecules, such as the 74-kDa protein. It is possible that this protein could be part of a putative receptor complex for dengue virus in Vero cells.

Cleavage of the 1, 2 isopropylidene acetal of 38 in refluxing 30 % aq AcOH provided the lactol 39, which was subjected to oxidative cleavage in CH 2 Cl 2 using sodium periodate furnishe[r]

beaker. In a second beaker, sodium periodate (0.6425 g, 0.003 mol) was dissolved in water (25 ml). The solutions were mixed and yellow crystals appeared after 1 h. The complex salt is sparingly soluble in acetone and fairly soluble in dimethylsulfoxide, but insoluble in chloroform. Elemental analysis, found: Co 12.64, C 10.40, H 4.00, N 18.05%; calculated for C 4 H 16 CoIN 6 O 8 : Co 12.76, C 10.38, H 3.46,

is pre-treated with sodium periodate, which selectively oxidizes sugar groups with vicinal hydroxyl groups. This finding strongly suggests that the ookinete binds to a midgut carbohydrate ligand. Ookinete adhesion is also reduced in the presence of total carbohydrates extracted from adult mosquitoes, suggesting competition for binding sites (Table 2). Furthermore, ookinete binding is reduced when the midguts are pre-treated with N-glycosidase A, which is a general N-glycosidase that hydrolyzes all types of N-glycans, even those with the α1,3-bound core fucose residues that are common in insect glycoproteins (Plummer et al., 1987; Tretter et al., 1991, 1993). Other general N-glycosidases (PNGase F, peptide N-glycosidase F) are sensitive to core fucosylation (Tretter et al., 1991) and do not reduce binding. As a result, we consider it likely that ookinetes bind to glycoproteins on the midgut surface that have a specific type of N-linked glycan unique to the midgut lumen and not found on the basement membranes of the midgut or other mosquito tissues.

Levels of anti-SjEA IgG was determined as described by ELISA [12]; whereas detection of anti-pSjEA IgG anti- bodies was performed with periodate treatment of egg antigens being carried out in plates as described [10]. Plates were coated overnight with 5 μg/ml of SjEA in carbonate-bicarbonate buffer (pH9.6). After being washed twice with 0.05 M sodium acetate (pH 4.6), 100 μl so- lutions containing 10 mM sodium-periodate dissolved in 0.05 M sodium acetate or containing 0.05 M so- dium acetate were added to SjEA coated in wells for 1 h at 37°C to make pSjEA. After washing plates with sodium acetate twice and with PBS once, the plates were treated with 50 mM sodium borohydride in PBS for 30 min at room temperature to stop periodate re- action. Mock-treated SjEA was subjected to the same procedure without sodium-periodate treatment. Plates were then extensively washed by PBS containing 0.05% Tween-20 (PBST) for 5 times and blocked with PBST containing 3% BSA for 1 h at 37°C. Sera or monoclo- nal antibodies were added at appropriate dilutions and incubated for 2 h at 37°C. After plates were washed with PBST, HRP-labeled goat anti-mouse IgG (H + L) was added at 1:10000 and incubated for another 1 h at 37°C. Final color development was achieved by addition of ABTS (2, 2′-Azino-bis (3-Ethylbenzthiazoline-6-Sulfonic Acid) (Sigma) with absorbance at 405 nm by plate reader (Thermo scientific) after plates being extensively washed.

In this study, Goat anti-Rabbit antibodies were labeled with Horseradish pe- roxidase using periodate oxidation method. Micro-concentration of HRP-Sodium Periodate solution was done to remove the excess of periodate in order to simpl- ify and accelerate the first step of conjugation. The reduction of the Schiff base of HRP-IgG conjugate by Sodium Borohydride was tested by incubating the solu- tion for 90 minutes and overnight before final dialysis of labeled Ab. The West- ern Blot and ELISA results showed no significant difference between conjugates stabilized for 90 minutes and overnight.

A simple, accurate and sensitive spectrophotometric way is used to determine Bisacodyl in pure and pharmaceutical preparations. The proposed method depends on using 2,4-Dinitrophenylhydrazine as chromogenic reagent . The method was based on the oxidative coupling reaction of Bisacodyl with 2,4-Dinitrophenylhydrazine with Sodium periodate in the presence of sodium hydroxide as alkaline media to form red water soluble dye product , that has a maximum absorption at λ max 522nm . Beer , s law is obeyed in the concentration of (2.00–20.00) μg.ml - 1 .The molar absorptivity is (6505) L.mol -1 .cm -1 ,a sandall sensitivity of(0.0555) μg.cm -2 ), correlation coefficient of (0.9970) , Limitof detection (LOD) (0.0312 μg.ml -1 ), limit of Quantitation (LOQ) (0. 3125 μg.ml -1

antigens on the cell surface, which are made of glycoproteins or glycolipids. 33-35 The terminal sugar residues of these glycoproteins or glycolipids are usually sialic acids and thus can be detected using the method developed above. To this end, cells that were incubated in a medium and allowed to divide were tested for the presence of sialic acids on their surfaces at 0,7,14 and 21 days. Using the procedure reported earlier for detecting sialic acids, the cells were subjected to mild periodate oxidation to selectively introduce aldehyde to the terminal sialic acids and subsequently tested for their ability to bind to our DAN-modified QCM chips. As shown in Fig. 3.5, no frequency shifts were observed at day zero, but frequency shift were observed in the subsequent measurements, increasing with the number of days of incubation. Also, the 40 k cells had higher frequency shifts that the 20 k cells for each measurement. Control reactions for the stem cell not treated with sodium periodate did not show any frequency shifts, indicating the binding was due to the introduction of aldehydes on the cell surface.

The effect of glycosylation on thermodynamic and kinetic properties of proteins is poorly studied now. However, a significant role of the carbohy - drate component in ensuring stability and in the processes of protein folding gains ever increasing corroboration in the works of recent years [11, 12]. And moreover, the works directed to increasing sta- bility by chemical glycosylation of proteins receive more and more recognition [13]. At the same time, deglycosylation of proteins can result both in insig - nificant changes of their properties and in complete loss of functional activity. Oxidation with sodium periodate permitted obtaining a modified form of C. cladosporioides α-galactosidase with low content of carbohydrate part (the amount of carbohydrates decreased to 3.2%, m/m). The modification resulting in the decrease of carbohydrates content to 2% and below was accompanied by practically complete loss of α-galactosidase activity.

[10] Mirkhani, V., Tangestaninejad, S., Moghadom, M. and Moghbel, M. (2004) Cy- tochrome P-450 Dependent Monooxygenases Model System: Rapid and Efficient Oxidation of Primary Aromatic Amines to Azo Derivatives with Sodium Periodate Catalyzed by Manganese(III) Schiff Base Complexes. Bioorganic & Medicinal Che- mistry , 12, 4673.

There are some reports on determination of Mn II based on periodate oxidation of some substrates [1-6]. A perusal of literature reveals that many methods that have been reported for determination of Mn I I are based on techniques such as titrimetry, spectrophotometry, pulse polarography, differential pulse anodic stripping voltametry, chromatography, flame atomic absorption spectroscopy, flow injection stopped flow spectrophotometry and Inductively coupled plasma optical emission spectrometry etc., and involve a complicated pre-treatment of samples, complex operation and use of costly equipments. Mn II catalysed periodate oxidation of aromatic amines has not been explored widely for kinetic-spectrophotometric estimation of Mn II and only a few attempts have been made in this direction[7-8], although there are some reports available in literature related to the Mn II catalysed/ uncatlysed periodate oxidation of aromatic amines[9-22]. In continuation to our kinetic mechanistic studies made on Mn II catalysed periodate oxidation of 2,4-xylidine[18], a new method developed by us for Mn II estimation based on its catalytic effect on the periodate oxidation of 2,4-xylidine (XYL), is being reported in present communication.

Determination of the linkages between carbohydrate and ribitol of the 6A ␤ repeating unit. To identify the 6A ␤ glucose that is periodate sensitive, we oxidized and reduced 6A ␤ PS, obtained repeating units by mild alkali hydrolysis, and studied the repeating units with tandem mass spectrometry. Their mass spectra showed several major (and dominant) peaks between m/z 650 and 700 (Fig. 4A). The dominant peaks were at m/z 655.23, 659.73, 661.24, 664.25, 673.25, and 675.24. Due to nat- ural isotopes, each dominant peak has satellite peaks with one or two additional mass units, and these satellite peaks can be FIG. 1. Antibody bound to ELISA plates (y axis) against the dilution of pneumococcal lysates (x axis). Lysates include two 6A ␤ isolates (solid symbols with continuous lines), three 6A ␣ isolates (open symbols with dotted lines), and two 6B isolates (dashed connecting lines). Antibodies used for the assay were Hyp6AG1 (A), Hyp6AM3 (B), rabbit serum pool Q (C), and rabbit “factor 6b” serum (D).

for six replicate determinations were 0.27% to 1.82% for the linear range of concentration 0.72 to 50.22 μg/mL. The absorbance maximum of the reaction mixture was recorded spectrophotometrically at 456nm. The method used for the determination of periodate in aqueous solutions was compared with the reported spectrophotometric methods. Various parameters related to the trace amount determination of periodate as molar absorptivity, Sandell’s sensitivity, initial rates of the reaction, percentage recovery and effect of interferrants etc. are being presented in this article.

To determine if cells dying by apoptosis were infected with PV, frozen longitudinal tissue sections 10 mm thick fixed in periodate-lysine-paraformaldehyde solution 20 were prepared from [r]

The study comprises oxidation of the battery samples containing manganese in lower oxidation state to manganese ( VII ) ( I ) by potassium periodate hot acid and ( ii ) by persulphate along with special reagents .The total manganese content in the samples analyzed were compared with those samples analyzed were compared with those values obtained by oxidizing standard manganese ( II ) sulfate ( known manganese content ) under similar conditions . So the values obtained in the present study may be considered suitable for the recovery of manganese.

treatment did not modify peptide epitopes). IgG antibodies against SWAP, SEAs, and ESPs produced before challenge largely bound to periodate-sensitive epitopes, whereas reactivity against periodate-resistant epitopes built up later in the course of the infection (figure 2C–2E). Of importance, treatment with periodate abrogated the reaction with 0–3-hRAP (figure 2F), thus revealing a close parallel with KLHg. The discrepancy between intact and periodate-treated antigen preparations re- vealed a gradation in the reactivity attributable to glycans (0–3- hRAP 1 SEAs 1 SWAP 1 ESPs). For all antigens tested, levels of protein-specific IgM antibodies were very low under the as- say conditions used (data not shown).

The effect of ALP on the rate of reaction was studied at constant concentrations of alkali, DPC and periodate at a constant ionic strength of 0.01 mol dm -3 in catalyzed reaction. In case of catalyzed reaction the ALP concentration was varied in the range of 1.0 x 10 -4 to 1.0 x 10 -3 mol dm -3 at 25 0 C while keeping other reactant concentrations and conditions constant. The K c values increased with the increase in concentration of ALP indicating an apparent less

A thorough literature survey of the various analytical methods for the quantitative estimation of Ornidazole in both bulk drug and dosage forms has revealed that very few analytical methods are available utilizing the hydrotropic solubilization technique to date. The present research paper is a descriptio n of a new analytical method developed using the principle of Hydrotropy employing very easily available chemical namely 1M Sodium benzoate solution. The method has been validated as per ICH guidelines and found to conform to ICH guidelines. In the present investigation the use of organic solvent has been avoided due to their high cost, volatility and toxicity , making the method environmental friendly. The findings revealed that the method is new, simple, safe, environmental friendly, accurate, precise, reproducible and cost-effective. It can be successfully employed as a routine analytical procedure for the analysis of Ornidazole tablets. Hence the authors suggest that this analytical method can be adopted in the Pharmaceutical industry for the analysis of Ornidazole in bulk and various dosage forms. . Ornidazole shows its maximum absorbance at 304 nm and Beer’s law was obeyed in concentration range of 2-5 µg/ml in presence of 1M Sodium benzoate and Molar absorptivity was computed as 0.0065934×10 3 mole -1 cm -1 . Sandell’s sensitivity was established as 0.0167 µg/cm 2 /0.001 abs.unit. Optimum photometric range was established from the Ringbom’s plot. The statistical analytical parameters namely Standard deviation and Correlation coefficient were computed and found to be 1.581, 0.996.