Efficient operation of a chemically pumped oxygen iodine laser utilizing dilute hydrogen peroxide

1987 ◽  
Vol 51 (19) ◽  
pp. 1490-1492 ◽  
Author(s):  
S. Yoshida ◽  
H. Fujii ◽  
T. Sawano ◽  
M. Endo ◽  
T. Fujioka
Keyword(s):  
Hydrogen Peroxide ◽  
Efficient Operation ◽  
Iodine Laser

Regeneration of basic hydrogen peroxide for chemical oxygen-iodine laser

2003 ◽  
Author(s):  
Masami Hano ◽  
Syuhei Wakita ◽  
Masaharu Uno ◽  
Masamori Endo ◽  
Kenzo Nanri ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Iodine Laser ◽  
Chemical Oxygen Iodine Laser ◽  
Basic Hydrogen Peroxide

Efficient operation of a Co : MgF2crystal laser pumped by radiation from a pulsed oxygen — iodine laser

1998 ◽  
Vol 28 (4) ◽  
pp. 288-289 ◽  
Author(s):  
Nikolai P Vagin ◽  
P G Kryukov ◽  
Yu P Podmar'kov ◽  
M P Frolov ◽  
Nikolai N Yuryshev
Keyword(s):  
Efficient Operation ◽  
Iodine Laser

Electrochemical regeneration of basic hydrogen peroxide for chemical oxygen iodine laser

2005 ◽  
Author(s):  
Masamori Endo ◽  
Masami Hano ◽  
Syuhei Wakita ◽  
Masaharu Uno ◽  
Shuzaburo Takeda
Keyword(s):  
Hydrogen Peroxide ◽  
Electrochemical Regeneration ◽  
Iodine Laser ◽  
Chemical Oxygen Iodine Laser ◽  
Basic Hydrogen Peroxide

scholarly journals Effect of Hydrogen Peroxide and Phosphate Addition on Biopolymers Formation and Changes in Head Loss in Biological Activated Carbon Process

2020 ◽  
Vol 42 (12) ◽  
pp. 654-663
Author(s):  
Heejong Son ◽  
Eun-Young Jung ◽  
Hee-Young Kim ◽  
Sang-Goo Kim
Keyword(s):  
Hydrogen Peroxide ◽  
Activated Carbon ◽  
Water Temperature ◽  
Concentration Ratio ◽  
Extracellular Polymeric Substances ◽  
Head Loss ◽  
Efficient Operation ◽  
Biological Activated Carbon ◽  
Cell Counts ◽  
The Stability

Objectives:The purpose of this study was to suggest a more efficient operation condition for the BAC(biological activated carbon) process by evaluating the change in the concentration of biopolymers in the effluent of the BAC process and the head loss of the BAC filter layer according to phosphate (PO4-P) and hydrogen peroxide (H2O2) input.Methods:During the experiment period (Feb. to Aug. 2020), the O3 dosage was fixed at 1 mg･O3/mg･DOC. Four columns with an inner diameter of 20 cm and a height of 250 cm were prepared. Empty bed contact time (EBCT) was fixed at 20 minutes and backwash was performed once a week. The four BAC columns are conventional BAC(control-BAC), enhanced BAC with hydrogen peroxide (H2O2+BAC), enhanced BAC with phosphate (PO4-P+BAC), and enhanced BAC with phosphate and hydrogen peroxide together (PO4-P+H2O2+BAC). In the case of enhanced BAC with PO4-P added, PO4-P was added with a concentration of 0.010 mg/L in the influent, and in BAC with H2O2, H2O2 was added with a concentration of 1 mg/L to the influent.Results and Discussion:According to the change of water temperature, the average head loss in control-BAC was 4.4 (25~28℃)~7.7 cm(8~12℃). In addition, PO4-P+BAC, H2O2+BAC and PO4-P+H2O2+BAC were 3.9~5.8 cm, 2.5~3.5 cm, and 2.6~3.5 cm, respectively. The head loss was reduced by the input of PO4-P and H2O2. During the low water temperature period, in control-BAC, the effluent biopolymers (BP) concentration was higher than the influent concentration, indicating that a large amount of EPS (extracellular polymeric substances) was produced and released from the attached biofilm. In PO4-P+BAC, H2O2+BAC and PO4-P+H2O2+BAC processes, the BP concentration ratio (Cout/Cin) was about 36~57% lower than that of the control-BAC during the low water temperature period. The BP concentration ratio was high when the water temperature (8~12℃) was low, and the BP concentration ratio gradually decreased as the water temperature increased. These results were very similar to those of the head loss change in the control-BAC process and the enhanced BAC process, and the BP concentration ratio and the head loss showed a very high correlation (r2=0.82~0.87). To evaluate the stability of the biofilm during the operation period, the total cell counts (TCC) in BAC treated waters were investigated. In control-BAC, PO4-P+BAC, H2O2+BAC and PO4-P+H2O2+BAC process, the average TCC was 46.8×106 cells, 30.3×106 cells, 21.8×106 cells, and 18.8×106 cells, respectively. Compared to the control-BAC, it was found to be 35~60% lower in the enhanced BAC processes. In addition, live cell count (LCC) ratio (LCC/TCC) was 0.84~0.89 in the enhanced BAC processes compared to 0.53 in the control-BAC. These results indicate that the biofilm stability of the enhanced BAC processes is higher than that of control-BAC.Conclusions:During the experiment, compared to the conventional BAC process, the enhanced BAC processes in which PO4-P and H2O2 were added showed a clear effect of reducing the head loss. In particular, the effect of reducing the head loss was higher when H2O2 was added than when PO4-P was added. A rapid head loss increase occurred in the conventional BAC process compared to the enhanced BAC processes in the low water temperature season is the result of the production of large amounts of EPS in the attached biofilm. The input of PO4-P or H2O2 reduces the head loss by improving the stability of the attached biofilm and reducing EPS production.

Chemical oxygen-iodine laser utilizing low-strength hydrogen peroxide

1984 ◽  
Vol 14 (8) ◽  
pp. 1138-1139 ◽  
Author(s):  
Nikolai P Vagin ◽  
A F Konoshenko ◽  
P G Kryukov ◽  
D Kh Nurligareev ◽  
V S Pazyuk ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Iodine Laser ◽  
Chemical Oxygen Iodine Laser ◽  
Low Strength

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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