PASTURE STUDIES. XXI.: AN IMPROVED THIOCHROME METHOD FOR THE ESTIMATION OF VITAMIN B1

1941 ◽  
Vol 19b (5) ◽  
pp. 136-142 ◽  
Author(s):  
W. D. McFarlane ◽  
R. A. Chapman
Keyword(s):  
Hydrogen Peroxide ◽  
Vitamin B1 ◽  
Optimum Amount

The thiochrome method as applied to foodstuffs by Pyke (10) has been modified to permit the use of the fluorimeter described by Froman and McFarlane (3). Interfering pigments are destroyed by adding hydrogen peroxide to the "blank" and test solutions before extracting with isobutanol. Hydrogen peroxide does not oxidize thiamine to thiochrome nor does it destroy the latter. The procedure described is based on a reinvestigation of the various methods proposed for extracting thiamine from tissues and also of the optimum amount of each reagent used in the thiochrome test.

scholarly journals A study on prediction method for ozone dosage and residual ozone concentration in advanced ozone water treatment

2017 ◽  
Vol 12 (1) ◽  
pp. 87-96 ◽  
Author(s):  
J. S. Hyung ◽  
K. B. Kim ◽  
M. C. Kim ◽  
I. S. Lee ◽  
J. Y. Koo
Keyword(s):  
Water Quality ◽  
Hydrogen Peroxide ◽  
Water Treatment ◽  
Environmental Factors ◽  
Real Time ◽  
Ozone Concentration ◽  
Prediction Method ◽  
Optimum Amount ◽  
Factors Affecting ◽  
Water Treatment Plants

Ozone dosage in most water treatment plants is operated by determining the ozone concentration with the experience of the operation. In this case, it is not economical. This study selected the factors affecting residual ozone concentration and attempted to estimate the optimum amount of hydrogen peroxide dosage for the control of the residual ozone concentration by developing a model for the prediction of the residual ozone concentration. The prediction formulas developed in this study can quickly respond to the environment of water quality and surrounding environmental factors, which change in real time, so it is judged that they could be used for the operation of the optimum ozone process, and the control of ozone dosage could be used as a new method in controlling the concentration of ozone dosage and the concentration of residual ozone.

scholarly journals Vitamin B1-Induced Priming Is Dependent on Hydrogen Peroxide and the NPR1 Gene in Arabidopsis

2006 ◽  
Vol 143 (2) ◽  
pp. 838-848 ◽  
Author(s):  
Il-Pyung Ahn ◽  
Soonok Kim ◽  
Yong-Hwan Lee ◽  
Seok-Cheol Suh
Keyword(s):  
Hydrogen Peroxide ◽  
Vitamin B1 ◽  
Npr1 Gene

scholarly journals Oxidation Desulphurization of Heavy Naphtha Improved by Ultrasound Waves

2020 ◽  
Vol 21 (1) ◽  
pp. 9-14
Author(s):  
Bariq Bahmman Jima ◽  
Najwa Saber Majeed
Keyword(s):  
Hydrogen Peroxide ◽  
Acetic Acid ◽  
Activated Carbon ◽  
Sulphur Content ◽  
Sonication Time ◽  
Optimum Amount ◽  
Ultrasound Waves ◽  
Oxidation Rates ◽  
Solid Adsorbent ◽  
Sulphur Removal

The oxidation desulphurization assisted by ultrasound waves was applied to the desulphurization of heavy naphtha. Hydrogen peroxide and acetic acid were used as oxidants, ultrasound waves as phase dispersion, and activated carbon as solid adsorbent. When the oxidation desulphurization (ODS) process was followed by a solid adsorption step, the performance of overall Sulphur removal was 89% for heavy naphtha at the normal condition of pressure and temperature. The process of (ODS) converts the compounds of Sulphur to sulfoxides/ sulfones, and these oxidizing compounds can be removed by activated carbon to produce fuel with low Sulphur content. The absence of any components (hydrogen peroxide, acetic acid, ultrasound waves and activated carbon) from the ODS process leading to reduce the performance of removal, hydrogen peroxide was the most crucial factor. The ultrasound waves increase the dispersion of carbon, water and oil phase, promotes the interfacial mass transfer, and this leads to accelerates the reaction. The ultrasound waves did not affect the chemical or physical properties of the fuel. The chemical analysis of treated fuel oil showed that <1% of the hydrocarbon fuel compounds were oxidized in the ODS process. In this work, desulphurization by oxidation is the main mechanism was tested with several parameters that effects desulphurization efficiency such as sonication time (5-40) min, activated carbon (0.01-0.5) gm, hydrogen peroxide (1-30) ml, and acetic acid (1-15) ml. It was found that the hydrogen peroxide amounts lead to increase oxidation rates of Sulphur compounds so, the desulphurization efficiency increases. The optimum amounts of oxidants are 10 ml hydrogen peroxide per 100 ml of heavy naphtha. Increasing the amount of acid catalyst lead to increase Sulphur removal, it was found that7.5 ml acid per 10 ml oxidant was the optimum amount. Activated carbon as a solid adsorbent and reaction enhancer with 0.1gm weight was found as the optimum amount for 100 ml heavy naphtha. Increasing sonication time lead to increase desulphurization rate, it was found that (10 min) is the optimum period. By applying the optimum parameters 89% of sulfur can be removed from heavy naphtha with 598.4 ppm Sulphur content.

Peroxidase Localization in Hartmanella Trophozoites

1971 ◽  
Vol 29 ◽  
pp. 346-347 ◽  
Author(s):  
George E. Childs ◽  
Joseph H. Miller
Keyword(s):  
Hydrogen Peroxide ◽  
Ultrastructural Localization ◽  
Pathogenic Strain ◽  
Oxidative Enzymes ◽  
Differential Centrifugation ◽  
Electron Microscopic ◽  
Microscopic Studies ◽  
The Subject ◽  
Axenic Cultures

Biochemical and differential centrifugation studies have demonstrated that the oxidative enzymes of Acanthamoeba sp. are localized in mitochondria and peroxisomes (microbodies). Although hartmanellid amoebae have been the subject of several electron microscopic studies, peroxisomes have not been described from these organisms or other protozoa. Cytochemical tests employing diaminobenzidine-tetra HCl (DAB) and hydrogen peroxide were used for the ultrastructural localization of peroxidases of trophozoites of Hartmanella sp. (A-l, Culbertson), a pathogenic strain grown in axenic cultures of trypticase soy broth.

Fluorescent proteins for in vivo imaging, where's the biliverdin?

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez
Keyword(s):  
Hydrogen Peroxide ◽  
In Vivo Imaging ◽  
Near Infrared ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Fluorescent Imaging ◽  
Infrared Light ◽  
Red Fluorescent Protein ◽  
Color Palette

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light &gt;600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.

Protective effect of chitooligosaccharides on hydrogen peroxide-induced PC-12 cells death by inhibition of oxidative damage

2010 ◽  
Vol 34 (8) ◽  
pp. S27-S27
Author(s):  
Xueling Dai ◽  
Ping Chang ◽  
Ke Xu ◽  
Changjun Lin ◽  
Hanchang Huang ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Oxidative Damage ◽  
Protective Effect ◽  
Pc 12 Cells ◽  
Cells Death

Signal-regulated oxidation of proteins via MICAL

2020 ◽  
Vol 48 (2) ◽  
pp. 613-620
Author(s):  
Clara Ortegón Salas ◽  
Katharina Schneider ◽  
Christopher Horst Lillig ◽  
Manuela Gellert
Keyword(s):  
Signal Transduction ◽  
Hydrogen Peroxide ◽  
Cell Death ◽  
Redox Regulation ◽  
Signal Transduction Pathways ◽  
Cellular Functions ◽  
Intracellular Signals ◽  
Amino Acid Side Chains ◽  
Specific Receptors ◽  
Sulfur Containing

Processing of and responding to various signals is an essential cellular function that influences survival, homeostasis, development, and cell death. Extra- or intracellular signals are perceived via specific receptors and transduced in a particular signalling pathway that results in a precise response. Reversible post-translational redox modifications of cysteinyl and methionyl residues have been characterised in countless signal transduction pathways. Due to the low reactivity of most sulfur-containing amino acid side chains with hydrogen peroxide, for instance, and also to ensure specificity, redox signalling requires catalysis, just like phosphorylation signalling requires kinases and phosphatases. While reducing enzymes of both cysteinyl- and methionyl-derivates have been characterised in great detail before, the discovery and characterisation of MICAL proteins evinced the first examples of specific oxidases in signal transduction. This article provides an overview of the functions of MICAL proteins in the redox regulation of cellular functions.

1223: Hydrogen Peroxide Induces Bladder Overactivity Via Sensitization of C-Fiber Afferent Pathways Through Activation of Cyclooxygenase in Rats

2005 ◽  
Vol 173 (4S) ◽  
pp. 332-332
Author(s):  
Hitoshi Masuda ◽  
Kazunori Kihara ◽  
Michael B. Chancellor ◽  
Naoki Yoshimura
Keyword(s):  
Hydrogen Peroxide ◽  
Afferent Pathways ◽  
C Fiber
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