scholarly journals The oxidation of sulphydryl compounds by hydrogen peroxide

1931 ◽  
Vol 25 (5) ◽  
pp. 1565-1579 ◽  
Author(s):  
Norman Wingate Pirie
Keyword(s):  
Hydrogen Peroxide ◽  
Sulphydryl Compounds

scholarly journals The oxidation of sulphydryl compounds by hydrogen peroxide

1933 ◽  
Vol 27 (4) ◽  
pp. 1181-1188 ◽  
Author(s):  
Norman Wingate Pirie
Keyword(s):  
Hydrogen Peroxide ◽  
Sulphydryl Compounds

Metabolic activities of sheep erythrocytes. II. Formate metabolism

1962 ◽  
Vol 13 (1) ◽  
pp. 45 ◽  
Author(s):  
RA Leng ◽  
EF Annison
Keyword(s):  
Carbon Dioxide ◽  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Aerobic Oxidation ◽  
Carbon Dioxide Production ◽  
Anaerobic Conditions ◽  
Formate Oxidation ◽  
Metabolic Activities ◽  
Sulphydryl Compounds ◽  
Formate Metabolism

Whole sheep blood, washed erythrocytes, and haemolysates showed only a slight capacity to oxidize 14C-labelled formate, as measured by labelled carbon dioxide production. Considerable oxidation of formate by washed erythrocytes or haemolysates occurred in the presence of systems generating hydrogen peroxide enzymically or non-enzymically under aerobic conditions. In addition, methylene blue was found to stimulate markedly the aerobic oxidation of formate by erythrocytes and haemolysates, the effect being abolished under anaerobic conditions. The stimulatory effects of methylene blue and sulphydryl compounds were additive. Evidence was obtained that the effect of methylene blue was mediated through an enzyme which directly or indirectly gave rise to hydrogen peroxide, formate oxidation being achieved by a hydrogen peroxide-catalase complex. No evidence was obtained of formate incorporation into red cells.

scholarly journals Oxidations by Hydrogen Peroxide in Presence of Sulphydryl Compounds

1927 ◽  
Vol 21 (3) ◽  
pp. 507-511
Author(s):  
Douglas Creese Harrison
Keyword(s):  
Hydrogen Peroxide ◽  
Sulphydryl Compounds

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.

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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