Amino Acid-Assisted Dehalogenation of Carbon Tetrachloride by Green Rust: Inhibition of Chloroform Production

2017 ◽  
Vol 51 (6) ◽  
pp. 3445-3452 ◽  
Author(s):  
Weizhao Yin ◽  
Bjarne W. Strobel ◽  
Hans Christian B. Hansen
Keyword(s):  
Amino Acid ◽  
Carbon Tetrachloride ◽  
Green Rust

Effects of Branched-Chain α-Keto Acids on Plasma Amino Acid Concentrations in Carbon Tetrachloride-Intoxicated Rats

1984 ◽  
Vol 114 (7) ◽  
pp. 1235-1241 ◽  
Author(s):  
Misako Okita ◽  
Akiharu Watanabe ◽  
Nobuyuki Takei ◽  
Hideo Nagashima ◽  
Toshihiko Ubuka
Keyword(s):  
Amino Acid ◽  
Carbon Tetrachloride ◽  
Plasma Amino Acid ◽  
Keto Acids ◽  
Branched Chain ◽  
Amino Acid Concentrations

Correction to “Efficient Dechlorination of Carbon tetrachloride by Hydrophobic Green Rust Intercalated with Dodecanoate Anions”

2012 ◽  
Vol 46 (8) ◽  
pp. 4683-4683 ◽  
Author(s):  
Karina B. Ayala-Luis ◽  
Nicola G. A. Cooper ◽  
Christian Bender Koch ◽  
Hans Christian B. Hansen
Keyword(s):  
Carbon Tetrachloride ◽  
Green Rust

Effects of AgI, AuIII, and CuIIon the Reductive Dechlorination of Carbon Tetrachloride by Green Rust

2003 ◽  
Vol 37 (13) ◽  
pp. 2905-2912 ◽  
Author(s):  
Edward J. O'Loughlin ◽  
Kenneth M. Kemner ◽  
David R. Burris
Keyword(s):  
Carbon Tetrachloride ◽  
Reductive Dechlorination ◽  
Green Rust

Synthesis of linear alkylbenzene sulphonate intercalated iron(II) iron(III) hydroxide sulphate (green rust) and adsorption of carbon tetrachloride

Clay Minerals ◽  
2007 ◽  
Vol 42 (3) ◽  
pp. 307-317 ◽  
Author(s):  
K. B. Ayala-Luis ◽  
D. K. Kaldor ◽  
C. Bender Koch ◽  
B. W. Strobel ◽  
H. C. B. Hansen
Keyword(s):  
Carbon Tetrachloride ◽  
Ion Exchange ◽  
Exchange Process ◽  
Green Rust ◽  
Stoichiometric Ratio ◽  
X Ray Diffraction ◽  
Linear Alkylbenzene ◽  
Ion Exchange Process ◽  
Linear Alkylbenzene Sulphonate ◽  
Kinetics Of

AbstractGreen rusts, GRs, can act as both sorbents and reductants towards selected pollutants. Organo-GRs are expected to combine these properties with a high affinity for hydrophobic substances. A novel organo-GR, GRLAS, was synthesized by incorporating a mixture of linear alkylbenzenesulphonates (LAS) into the interlayer space of synthetic sulphate green rust, GRSO4 . Mössbauer analysis of GRLAS indicates that the structure of the organo-GR is very similar to that of the initial GRSO4 with regard to the FeII/FeIII ratio and local coordination of Fe atoms. X-ray diffraction demonstrates that the GRLAS formed was well ordered, although a mixture of surfactant was used for intercalation. The basal spacings of the GRLAS and the kinetics of the ion-exchange process were dependent on the initial surfactant loading; basal spacings of ~2.85 nm were obtained at LAS solution concentrations >10 mM. The ratio LASadsorbed/SO42–desorbed significantly exceeded the stoichiometric ratio of 2 during the initial part of the ion-exchange process (t = 5 h). However, this ratio was reached progressively with time. GRSO4 preferentially sorbed LAS homologues with long alkyl chains over short ones. Carbon tetrachloride was successfully adsorbed into GRLAS. The adsorption isotherm was linear with a distribution coefficient, Kd, of 505±19 litre kg–1.

scholarly journals AN INTRACELLULAR DEFECT IN PROTEIN SYNTHESIS INDUCED BY CARBON TETRACHLORIDE

1962 ◽  
Vol 116 (1) ◽  
pp. 55-72 ◽  
Author(s):  
Edward A. Smuckler ◽  
Oscar A. Iseri ◽  
Earl P. Benditt
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Carbon Tetrachloride ◽  
Morphological Changes ◽  
Succinic Dehydrogenase ◽  
Metabolic Effects ◽  
Amino Acid Incorporation ◽  
Functional Changes ◽  
Acid Incorporation ◽  
Carbon Tetrachloride Administration

The morphological and certain metabolic effects of carbon tetrachloride intoxication were studied in the rat with emphasis on liver alterations. Morphological changes were investigated by histological and electron microscopical means. Functional changes were investigated using histochemical and amino acid incorporation, techniques. The liver constituents were examined chemically. Plasma volume alterations were measured using dye and homologous protein dilution techniques. The histological appearance of the liver of treated animals included cellular swelling, dispersal of the cytoplasmic basophilia, and necrosis. Electron micrographs showed an early (3 hours following carbon tetrachloride administration) and widespread dislocation of the ribonucleoprotein particles from the membranes of the rough endoplasmic reticulum, but no apparent alteration in the mitochondrial structure. Histochemical examination of two mitochondrial enzyme systems, α-ketoglutarate dehydrogenase and succinic dehydrogenase, revealed no alterations in activities until a later time (6 to 12 hours following carbon tetrachloride administration). ATPase showed a gross quantitative decrease in activity at 6 and 12 hours, but not earlier. There was a decreased amino acid incorporation into two liver-produced proteins, viz., albumin and fibrinogen. This decrease is not explicable on the basis of the inability of the liver to take up the amino acid, an altered dilution volume into which the amino acid or formed protein is placed, or an impaired capacity of the liver to excrete protein once formed. It is concluded that the decreased amino acid incorporation rate reflects depressed synthesis of protein by the liver. Other pathological changes in the liver, including necrosis, fatty change, and mitochondrial alterations may be dependent upon severe impairment of protein synthesis.

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