PROMOTER ACTION IN HOMOGENEOUS CATALYSIS. IV. DECOMPOSITION OF HYDROGEN PEROXIDE BY POTASSIUM DICHROMATE ACCELERATED BY MANGANESE SALTS

1927 ◽  
Vol 49 (7) ◽  
pp. 1630-1642 ◽  
Author(s):  
Alfred C. Robertson
Keyword(s):  
Hydrogen Peroxide ◽  
Homogeneous Catalysis ◽  
Potassium Dichromate ◽  
Manganese Salts

Preparing Diatoms for EM

2000 ◽  
Vol 8 (9) ◽  
pp. 36-37
Author(s):  
Greg Strout
Keyword(s):  
Electron Microscopy ◽  
Hydrogen Peroxide ◽  
Scanning Electron Microscopy ◽  
Diatomaceous Earth ◽  
Potassium Dichromate ◽  
Scanning Electron

Diatoms make for beautiful specimens for both transmission and scanning electron microscopy. As well, they are studied by many people, and there is always a need for good diatom preparations for EM.I find that the diatoms in diatomaceous earth are usually broken, and like to prepare my own from fresh specimens. The materials needed for this are a plankton net, some potassium dichromate, and 30% hydrogen peroxide. Once the diatoms are collected (plankton net tows from shoreline, or wherever), they can be cleaned using the chemicals.

scholarly journals Comparison of Landfill Leachate Treatment Efficiency Using the Advanced Oxidation Processes

2013 ◽  
Vol 39 (2) ◽  
pp. 107-115 ◽  
Author(s):  
Barbara Pieczykolan ◽  
Izabela Płonka ◽  
Krzysztof Barbusiński ◽  
Magdalena Amalio-Kosel
Keyword(s):  
Hydrogen Peroxide ◽  
Organic Compounds ◽  
Advanced Oxidation Processes ◽  
Potassium Dichromate ◽  
Advanced Oxidation ◽  
Fenton’S Reagent ◽  
Nitrogen And Phosphorus ◽  
Leachate Treatment ◽  
Fenton's Reagent ◽  
Oxidation Processes

Abstract Treatment of leachate from an exploited since 2004 landfill by using two methods of advanced oxidation processes was performed. Fenton’s reagent with two different doses of hydrogen peroxide and iron and UV/H2O2 process was applied. The removal efficiency of biochemically oxidizable organic compounds (BOD5), chemically oxidizable compounds using potassium dichromate (CODCr) and nutrient (nitrogen and phosphorus) was examined. Studies have shown that the greatest degree of organic compounds removal expressed as a BOD5 index and CODCr index were obtained when Fenton’s reagent with greater dose of hydrogen peroxide was used - efficiency was respectively 72.0% and 69.8%. Moreover, in this case there was observed an increase in the value of ratio of BOD5/CODCr in treated leachate in comparison with raw leachate. Application of Fenton’s reagent for leachate treatment also allowed for more effective removal of nutrients in comparison with the UV/H2O2 process.

Antigenotoxic properties of selenium compounds on potassium dichromate and hydrogen peroxide

2003 ◽  
Vol 23 (S2) ◽  
pp. 53-67 ◽  
Author(s):  
Eduardo Cemeli ◽  
Joanna Carder ◽  
Diana Anderson ◽  
Emma Guillamet ◽  
Mar�a Jos� Morillas ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Potassium Dichromate ◽  
Selenium Compounds

Preparation of Thin Cadmium Telluride Samples for Electron Microscope Studies

1974 ◽  
Vol 32 ◽  
pp. 548-549
Author(s):  
T. J. Magee ◽  
J. Peng ◽  
J. Bean
Keyword(s):  
Electron Microscope ◽  
Sulfuric Acid ◽  
Solid State ◽  
Sample Preparation ◽  
Cadmium Telluride ◽  
Potassium Dichromate ◽  
Optical Components ◽  
The Past ◽  
Solid State Devices

Cadmium telluride has become increasingly important in a number of technological applications, particularly in the area of laser-optical components and solid state devices, Microstructural characterizations of the material have in the past been somewhat limited because of the lack of suitable sample preparation and thinning techniques. Utilizing a modified jet thinning apparatus and a potassium dichromate-sulfuric acid thinning solution, a procedure has now been developed for obtaining thin contamination-free samples for TEM examination.

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 >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.

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