Fast Detection of Nitrite with a Test Paper Tape

2012 ◽  
Vol 538-541 ◽  
pp. 2181-2183
Author(s):  
Bao Shan He ◽  
Fang Wei ◽  
Na Gao ◽  
Qi Yu Lu
Keyword(s):  
Sulfanilic Acid ◽  
Paper Tape ◽  
Testing Time ◽  
Dependent Manner ◽  
Test Paper ◽  
Concentration Dependent Manner ◽  
Fast Detection ◽  
System A ◽  
Ethylenediamine Dihydrochloride

A test paper tape on the determination of nitrite in food was designed, which is based on the diazotization of nitrite with sulfanilic acid under weakly acidic conditions then coupled with N-(1-Naphthyl)-ethylenediamine dihydrochloride in forming the colour-producing response. Then the reaction membrane turned to purple-red. The deeper purple-red film was obtained in an increased nitrite concentration-dependent manner. Experimental results showed that nitrite concentrations were proportional to a values of the L a b color system. A favorable linearity was presented in the range of 25 to 5000 μg/mL. The correlation coefficient(r) was 0.984 and the whole testing time needed was about 1.5 min at room temperature.

scholarly journals Ghrelin Alleviates Endoplasmic Reticulum Stress in MC3T3E1 Cells by Inhibiting AMPK Phosphorylation

2021 ◽  
Vol 2021 ◽  
pp. 1-14
Author(s):  
Xue Lv ◽  
Qianping Zhang ◽  
Bingfei Cheng ◽  
Ying Xin ◽  
Jun Wang ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Energy Homeostasis ◽  
Marker Genes ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Expression Of Genes ◽  
Species Production ◽  
Related Proteins

Ghrelin is a gastric endocrine peptide that has been found to be involved in the process of energy homeostasis and bone physiology in recent years. To explore the effects of ghrelin on endoplasmic reticulum stress (ERS) in MC3T3E1 cells and its possible mechanism, an ERS model was induced by tunicamycin (TM) in the osteoblast line MC3T3E1. TM at 1.5 μg/mL was selected as the experimental concentration found by CCK8 assay. Through the determination of apoptosis, reactive oxygen species production, and endoplasmic reticulum stress-related gene expression, we found that ERS induced by TM can be relieved by ghrelin in a concentration-dependent manner ( P < 0.001 ). Compared with the TM group, ghrelin reduced the expression of ERS-related marker genes induced by TM. Compared with the GSK621 + TM group without ghrelin pretreatment, the mRNA expression of genes in the ghrelin pretreatment group decreased significantly ( P < 0.001 ). The results of protein analysis showed that the levels of BIP, p-AMPK, and cleaved-caspase3 in the TM group increased significantly, while the levels decreased after ghrelin pretreatment. In group GSK621 + TM compared with group GSK621 + ghrelin+TM, ghrelin pretreatment significantly reduced the level of p-AMPK, which is consistent with the trend of the ERS-related proteins BIP and cleaved-caspase3. In conclusion, ghrelin alleviates the ERS induced by TM in a concentration-dependent manner and may or at least partly alleviate the apoptosis induced by ERS in MC3T3E1 cells by inhibiting the phosphorylation of AMPK.

Effects of inhibition of myo-inositol transport on MDCK cells under hypertonic environment

1997 ◽  
Vol 272 (2) ◽  
pp. F267-F272 ◽  
Author(s):  
H. Kitamura ◽  
A. Yamauchi ◽  
T. Nakanishi ◽  
Y. Takamitsu ◽  
T. Sugiura ◽  
...  
Keyword(s):  
Mdck Cells ◽  
Competitive Inhibitor ◽  
Maximal Velocity ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
System A ◽  
Neutral Amino Acid Transporter ◽  
Colony Forming Efficiency ◽  
Dependent Component ◽  
Forming Efficiency

To investigate the role of myo-inositol under hypertonic conditions, we examined the effects of inhibition of myo-inositol transport in Madin-Darby canine kidney (MDCK) cells using an analog of myo-inositol, 2-O,C-methylene-myo-inositol (MMI). We first characterized the inhibitory effects of MMI on myo-inositol transport in MDCK cells. The Na+-dependent component of [3H] myo-inositol uptake was inhibited by MMI in a concentration-dependent manner, although MMI did not inhibit the activities of the betaine transporter and system A neutral amino acid transporter. We found decreased affinity for myo-inositol in the presence of MMI, whereas the maximal velocity (Vmax) of the transporter did not change. Thus MMI behaves as a competitive inhibitor of myo-inositol transport with a relatively high inhibition constant (K(i)) value (1.6 mM). Myo-inositol content in hypertonic MDCK cells was markedly reduced in the presence of 5 mM MMI, but MMI itself did not accumulate in these cells. The hypertonic cells began to detach in the presence of MMI 3 days after increasing medium osmolality, whereas MMI did not affect the cells in isotonic medium. We also examined the effects of MMI on colony-forming efficiency of MDCK cells. MMI decreased colony-forming efficiency in a concentration-dependent manner, and addition of myo-inositol returned the efficiency to the value without MMI. Addition of betaine also increased colony-forming efficiency in the presence of MMI. These results indicate that myo-inositol plays an important role in survival and growth under hypertonic environment.

Canine jejunal submucosa cultures: characterization and release of neural somatostatin

1990 ◽  
Vol 68 (6) ◽  
pp. 705-710 ◽  
Author(s):  
A. M. J. Buchan ◽  
A. D. Doyle ◽  
E. Accili
Keyword(s):  
Substance P ◽  
Calcium Ionophore ◽  
Calcium Ionophore A23187 ◽  
Neuronal Cultures ◽  
Ionophore A23187 ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Cell Content ◽  
Cell Extracts

A primary culture of the canine jejunal submucosa has been established and used to investigate neuronal somatostatin release. Immunocytochemical characterization of the cultures demonstrated the presence of the following peptidergic neurons: neurotensin (30%), somatostatin (27%), vasoactive intestinal polypeptide (14%), neuropeptide Y (10%), and substance P (5%). No immunoreactive neurons were observed with the available antisera to galanin, gastrin-releasing peptide, and motilin. The concentration of somatostatin-like immunoreactivity, as determined by radioimmunoassay of cell extracts, was 358 ± 105 pmol/well. Basal release of somatostatin was 4.4 ± 0.9% total cell content and was significantly inhibited by the addition of substance P at 1 and 100 nM. The addition of the calcium ionophore, A23187, with phorbol 12-myristate 13-acetate stimulated somatostatin release in a concentration-dependent manner. These data indicate that short-term cultures of the jejunal submucosal plexus will be an excellent model for determination of the factors influencing the release of neural somatostatin.Key words: immunocytochemistry, neuronal cultures, neurofilament, substance P.

scholarly journals Antiadipogenic Effects ofAster glehniExtract: In Vivo and In Vitro Effects

2013 ◽  
Vol 2013 ◽  
pp. 1-10 ◽  
Author(s):  
Heon-Myung Lee ◽  
Gabsik Yang ◽  
Tae-Gue Ahn ◽  
Myung-Dong Kim ◽  
Agung Nugroho ◽  
...  
Keyword(s):  
Therapeutic Potential ◽  
Control Diet ◽  
Epididymal Adipose Tissue ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Master Regulators ◽  
In Vitro Effects

Aster glehni(AG) is a Korean traditional herb that grows in Ulleungdo Island, Republic of Korea. None of the several reports on AG include a determination of the effect of AG on adipogenesis. The primary aim of this study was to determine whether AG attenuates adipogenesis in mouse 3T3-L1 cells and epididymal fat tissue. AG blocked the differentiation of 3T3-L1 preadipocytes in a concentration-dependent manner and suppressed the expression of adipogenesis-related genes such asPPARγ,C/EBPα, andSREBP1c, the master regulators of adipogenesis. Male C57BL/6J mice were divided randomly and equally into 4 diet groups: control diet (CON), high-fat diet (HFD), HFD with 1% AG extract added (AG1), and HFD with 5% AG extract added (AG5). The experimental animals were fed HFD and the 2 combinations for 10 weeks. Mice fed HFD with AG gained less body weight and visceral fat-pad weight than did the mice fed HFD alone. Moreover, AG inhibited the expression of important adipogenic genes such asPPARγ,C/EBPα,SREBP1c,LXR, and leptin in the epididymal adipose tissue of the mice treated with AG1 and AG5. These findings indicate antiadipogenic and antiobesity effects of AG and suggest its therapeutic potential in obesity and obesity-related diseases.

scholarly journals Evidence for allosteric regulation of pH-sensitive System A (SNAT2) and System N (SNAT5) amino acid transporter activity involving a conserved histidine residue

2006 ◽  
Vol 397 (2) ◽  
pp. 369-375 ◽  
Author(s):  
Fiona E. Baird ◽  
Jorge J. Pinilla-Tenas ◽  
William L. J. Ogilvie ◽  
Vadival Ganapathy ◽  
Harinder S. Hundal ◽  
...  
Keyword(s):  
Amino Acid ◽  
Mammalian Cells ◽  
Ph Sensitivity ◽  
Amino Acid Transporters ◽  
Dependent Manner ◽  
Histidine Residue ◽  
Concentration Dependent Manner ◽  
Histidine Residues ◽  
System A ◽  
External Ph

System A and N amino acid transporters are key effectors of movement of amino acids across the plasma membrane of mammalian cells. These Na+-dependent transporters of the SLC38 gene family are highly sensitive to changes in pH within the physiological range, with transport markedly depressed at pH 7.0. We have investigated the possible role of histidine residues in the transporter proteins in determining this pH-sensitivity. The histidine-modifying agent DEPC (diethyl pyrocarbonate) markedly reduces the pH-sensitivity of SNAT2 and SNAT5 transporters (representative isoforms of System A and N respectively, overexpressed in Xenopus oocytes) in a concentration-dependent manner but does not completely inactivate transport activity. These effects of DEPC were reversed by hydroxylamine and partially blocked in the presence of excess amino acid substrate. DEPC treatment also blocked a reduction in apparent affinity for Na+ (K0.5Na+) of the SNAT2 transporter at low external pH. Mutation of the highly conserved C-terminal histidine residue to alanine in either SNAT2 (H504A) or SNAT5 (H471A) produced a transport phenotype exhibiting reduced, DEPC-resistant pH-sensitivity with no change in K0.5Na+ at low external pH. We suggest that the pH-sensitivity of these structurally related transporters results at least partly from a common allosteric mechanism influencing Na+ binding, which involves an H+-modifier site associated with C-terminal histidine residues.

scholarly journals Selenium-containing amino acids are targets for myeloperoxidase-derived hypothiocyanous acid: determination of absolute rate constants and implications for biological damage

2011 ◽  
Vol 441 (1) ◽  
pp. 305-316 ◽  
Author(s):  
Ojia Skaff ◽  
David I. Pattison ◽  
Philip E. Morgan ◽  
Rushad Bachana ◽  
Vimal K. Jain ◽  
...  
Keyword(s):  
Rate Constants ◽  
Hypochlorous Acid ◽  
Thioredoxin Reductase ◽  
Kinetic Studies ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Biological Damage ◽  
Hypobromous Acid ◽  
Protective Enzymes

Elevated MPO (myeloperoxidase) levels are associated with multiple human inflammatory pathologies. MPO catalyses the oxidation of Cl−, Br− and SCN− by H2O2 to generate the powerful oxidants hypochlorous acid (HOCl), hypobromous acid (HOBr) and hypothiocyanous acid (HOSCN) respectively. These species are antibacterial agents, but misplaced or excessive production is implicated in tissue damage at sites of inflammation. Unlike HOCl and HOBr, which react with multiple targets, HOSCN targets cysteine residues with considerable selectivity. In the light of this reactivity, we hypothesized that Sec (selenocysteine) residues should also be rapidly oxidized by HOSCN, as selenium atoms are better nucleophiles than sulfur. Such oxidation might inactivate critical Sec-containing cellular protective enzymes such as GPx (glutathione peroxidase) and TrxR (thioredoxin reductase). Stopped-flow kinetic studies indicate that seleno-compounds react rapidly with HOSCN with rate constants, k, in the range 2.8×103–5.8×106 M−1·s−1 (for selenomethionine and selenocystamine respectively). These values are ~6000-fold higher than the corresponding values for H2O2, and are also considerably larger than for the reaction of HOSCN with thiols (16-fold for cysteine and 80-fold for selenocystamine). Enzyme studies indicate that GPx and TrxR, but not glutathione reductase, are inactivated by HOSCN in a concentration-dependent manner; k for GPx has been determined as ~5×105 M−1·s−1. Decomposed HOSCN did not induce inactivation. These data indicate that selenocysteine residues are oxidized rapidly by HOSCN, with this resulting in the inhibition of the critical intracellular Sec-dependent protective enzymes GPx and TrxR.

scholarly journals EFFECT OF HARVESTING TIME AT MORNING, AFTERNOON, AND EVENING ON NITRATE AND NITRITE LEVEL IN SPINACH (AMARANTHUS TRICOLOR L.) AND MUSTARD (BRASSICA RAPA L.)

2018 ◽  
Vol 11 (13) ◽  
pp. 110
Author(s):  
Nahitma Ginting ◽  
Jansen Silalahi ◽  
Tuty Roida Pardede ◽  
Sudarmi Sudarmi ◽  
Nerdy Nerdy
Keyword(s):  
Research Result ◽  
Reduction Process ◽  
Sulfanilic Acid ◽  
Harvesting Time ◽  
Nitrite Level ◽  
Nitrate Determination ◽  
Acid Reagent ◽  
Ethylenediamine Dihydrochloride ◽  
Nitrate And Nitrite

 Objective: The objective of this study is to determine the effect of harvesting time at morning, afternoon, and evening on nitrate and nitrite level in spinach and mustard.Methods: Nitrite identification was done using sulfanilic acid reagent and N-(1-naphthyl) ethylenediamine dihydrochloride. Identification of nitrate was done using reagent ferrous sulfate. Determination of nitrites level was performed visible spectrophotometry using N-(1-naphthyl) ethylenediamine dihydrochloride at maximum wavelength of 540 nm. Nitrate determination is taken with the same method but started with reduction process from nitrate into nitrite using Zn powder in acid condition and then measured as nitrite.Results: Research result shows that there is a change of nitrate and nitrite level from the spinach harvested at morning, afternoon, and evening.Conclusion: Spinach and mustard are better harvested in the morning because it contains nitrite less than in spinach picked afternoon and evening. Level of nitrite increases from morning to afternoon and decreases from afternoon to evening. However, the level of nitrate decreases from morning to afternoon and increases from afternoon to evening.

The Point of Care Monitor Coagucheck-XS Displays the Lowest Coefficient of Variation for Determination of Rivaroxaban Compared to Prothrombin Time and Chromogenic Assays,

Blood ◽  
2011 ◽  
Vol 118 (21) ◽  
pp. 3353-3353
Author(s):  
Job Harenberg ◽  
Christina Giese ◽  
Svetlana Marx
Keyword(s):  
Whole Blood ◽  
Point Of Care ◽  
Improve Patient Care ◽  
Rabbit Brain ◽  
P Value ◽  
Dependent Manner ◽  
Intraindividual Variation ◽  
Concentration Dependent Manner ◽  
Coagulation Assays

Abstract Abstract 3353 The new oral direct coagulation inhibitor rivaroxaban prolongs coagulation times of various coagulation assays in a concentration-dependent manner. A point of care determination of the anticoagulant effect of rivaroxaban would improve patient care and patient's safety in case of overdose of rivaroxaban. We have analysed intraindividual coefficients of variations (CV) of the Coagucheck XS compared to the STA Neoplastin Plus and STA Rotachrom heparin assays. Rivaroxaban was spiked to whole blood and plasma from 10 healthy donors (50ng/ml, 200 ng/ml, and 600 ng/ml). Coagulation times and ratios were measured by means of the Coagucheck XS (recombinant human thromboplastin) from whole blood and plasma samples and STA Neoplastin Plus (rabbit brain thromboplastin). The concentration of rivaroxaban was determined using the factor Xa specific chromogenic substrate STA Rotachrom heparin assay. The intraindividual CVs were calculated from 10 determinations at 10 days for the methods at all concentrations of rivaroxaban. Rivaroxaban prolonged coagulation times of all coagulation assays. The ratios increased from 0 ng/ml to 600 ng/ml rivaroxaban from 1.0 (50 ng/ml) to 1.20 (200 ng/ml) and 1.63 (600 ng/ml) using the whole blood Coagucheck XS method, from 1.0 to 1.33 to 1.85 using plasma on Coagucheck XS, and from 1.0 to 1.51 to 1.80 using the STA Neoplastin Plus assay, respectively. Values of the STA Rotachrom assay were used for comparison of the CVs of the methods. CVs were calculated from the original data (seconds or optical density). CVs were calculated from the intraindividual variation over 10 days for every volunteer. The median, minimum and maximum values are displayed as well as the p-value for the difference of the CVs between methods for every concentration of rivaroxaban (Kruskal Wallis test).MethodRivaroxaban: 0ng/ml50ng/ml200ng/ml600ng/mlCogucheck XSCV median1.040.991.040.87whole bloodmin-max0.38–1.700.65–1.430.37–1.680.40–1.40Coagucheck XSCV median1.081.011.041.80plasmamin-max0.83–2.380.46–2.800.61–2.360.52–3.17Neoplastin PlusCV median1.831.743.974.30min-max1.06–2.171.33–2.671.75–4.832.02–6.09RotachromCV median1.481.843.972.99min-max0.96–2.390.97–2.392.46–6.492.08–6.15p-value0.01150.0011<.0001<.0001 The point of care monitor Coagucheck XS using whole blood determines with the highest accuracy and precision the amount of rivaroxaban. The method may be used to screen for overdose in patients on treatment with rivaroxaban. Disclosures: Harenberg: Roche Diagnostics: Research Funding.

scholarly journals The Effect of Boiling Time and the Type of Utensil Used on the Nitrite and Nitrate Contents in Carrots (Daucus carota L.)

2018 ◽  
Vol 1 (1) ◽  
pp. 18-27 ◽  
Author(s):  
Jansen Silalahi ◽  
Shena Keshia Aritonang ◽  
Muchlisyam
Keyword(s):  
Stainless Steel ◽  
Sulfanilic Acid ◽  
Zinc Powder ◽  
Nitrate Level ◽  
Daucus Carota L ◽  
Nitrite Level ◽  
Ethylenediamine Dihydrochloride ◽  
Nitrate And Nitrite ◽  
North Sumatra

Abstract.  The purpose of this study was to investigate the effect of boiling time using utensils made of different metal component on thenitrate and nitrite contentsin carrots. The carrots were obtained from Jaranguda Village, Karo Regency, North Sumatra. The utensil types used for boiling were made of stainless steel, what so called periuk and aluminum and boiling time were 5 minutes, 10 minutes and 15 minutes.The determination of nitrite was done by visible spectrophotometer using sulfanilic acid and N-(1-naphthyl) ethylenediamine dihydrochloride reagentsand absorbance was measured at a wavelength of 540 nm. The determinationof nitrate wascarried out by reducing the nitrate into nitrite using Zinc powder and diluted HCl then measured as nitrite. The nitritelevel was then convertedinto nitrate. The result showed that the utensil types and boiling time affected the levels of nitrate and nitrite in carrots. The nitrate and nitrite levels in fresh carrots was 32.14 mg/kg and 24.78 mg/kg respectively. After boiling for 5 minutes, the nitrate and nitrite levels decreased significantly. Further boiling of boiled carrots, the nitrite levelincreased in the aluminum utensil from 11.00 mg/kg to 20.15 mg/kg (83 %); in periuk from 9.18 mg/kg to 16.95 mg/kg (78%) andin stainless steelfrom 8.21 mg/kg to 11.75 mg/kg (43%). While the nitrate level decreased in aluminumutensil from 27.14 mg/kg to 21.08 mg/kg (22%); stainless steel from 16.40 mg/kg to 13.25 mg/kg (19%) and periuk from 20.30 mg/kg to 16.51 mg/kg (18%).  The results of this study indicated that the nitrite level increased, while nitrate level decreased with boiling time.The effect of utensil type used on boiling increased nitrite but decreased nitrate level in carrotsand these effects were found that the mostinfluential treatmentwas using utensil made of aluminum. Keyword: Carrot, Boiling Time, Nitrate, Nitrit, Utensil Type

scholarly journals Cyclopentadione-aniline conjugate suppresses proliferation and induces apoptosis in liver cancer cells via up-regulation of p38 phosphorylation

2021 ◽  
Vol 18 (3) ◽  
pp. 505-511
Author(s):  
Heze Yu ◽  
Geao Liang ◽  
Bo Dou ◽  
Jiangdong Ni
Keyword(s):  
Liver Cancer ◽  
Cancer Cells ◽  
Hepg2 Cells ◽  
Dependent Manner ◽  
Transwell Assay ◽  
Invasive Potential ◽  
Concentration Dependent Manner ◽  
Liver Cancer Cells ◽  
Proliferation And Apoptosis

Purpose: To investigate the effect of cyclopentadione-aniline conjugate (CAC) on proliferation of liver cancer cells. Methods: MTT assay and flow cytometry were used for the determination of the effect of CAC on cell proliferation and apoptosis. Western blotting was used to measure the influence of CAC on the expressions of various proteins, while Matrigel-coated Transwell assay was used for assessment of cell invasion. Results: CAC inhibited proliferation of liver cancer cells in a concentration-dependent manner. The degree of proliferation of HepG2 cells was 98, 89, 76, 66, 51, 42 or 36 %, on treatment with 0.25, 0.5, 1.0, 1.5, 2.0, 2.5 or 3.0 µM CAC, respectively. In H4TG cells, treatment with 0.25, 0.5, 1.0, 1.5, 2.0, 2.5 and 3.0 µM CAC decreased proliferation of cells to 99, 91, 79, 70, 54, 46 and 40 %, respectively. Apoptosis was induced in 34.56, 37.37 and 52.98 % cells, on treatment with 2.0, 2.5 and 3.0 µM CAC, respectively. The invasive potential of HepG2 cells was significantly decreased by CAC (p < 0.05). Marked decreases were observed in Bcl-2, MMP-2, MMP-9, c-ERK1/2 and phospho-Akt levels in CACtreated HepG2 cells. CAC treatment markedly upregulated Bax and phospho ERK1/2, but significantly downregulated phospho PI3K, phospho mTOR and phospho Akt in HepG2 cells (p < 0.05). However, the level of phospho p38 was decreased in CAC-treated cells. Conclusion: These results demonstrate that CAC inhibits proliferation of liver cancer cells via apoptosis induction. Thus, CAC can potentially be used for the treatment of liver cancer in humans

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