Results 171 to 180 of about 6,015 (201)
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Active site peptides of rhodanese
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1970Abstract The active site cysteinyl peptide isolated from a tryptic digest of rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1) by column chromatography has been found to contain 15 amino acid residues, of which 7 are hydrophobic. The tryptophyl peptides in such digests also appear to consist predominantly of residues which are hydrophobic.
F, Detoma, J, Westley
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Biochemical and Biophysical Research Communications, 1971
Abstract The binding of zinc ion to bovine beef liver rhodanese has been investigated by nuclear magnetic resonance and emission spectroscopic methods. One equivalent of zinc ion is found to bind strongly to the enzyme; however, zinc is absent in the fully active native enzyme and the addition of zinc ion does not enhance catalytic activity.
R G, Bryant, S, Rajender
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Abstract The binding of zinc ion to bovine beef liver rhodanese has been investigated by nuclear magnetic resonance and emission spectroscopic methods. One equivalent of zinc ion is found to bind strongly to the enzyme; however, zinc is absent in the fully active native enzyme and the addition of zinc ion does not enhance catalytic activity.
R G, Bryant, S, Rajender
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Rhodanese as a thioredoxin oxidase
The International Journal of Biochemistry & Cell Biology, 2000A major catalytic difference between the two most common isoforms of bovine liver mitochondrial rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) has been observed. Both isoforms were shown to be capable of using reduced thioredoxin as a sulfur-acceptor substrate.
D L, Nandi, P M, Horowitz, J, Westley
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The activity of avian Rhodanese
British Poultry Science, 1977A survey of rhodanese activity (thiosulphate: cyanide sulphur transferase) in the tissues of the domestic fowl revealed that the highest activity occurred in the kidney, approximately twice that in the liver, 316 and 141 mumol SCN formed/min g protein, respectively. 2. In sparrows, pigeons and ducks, liver and kidney activities tended to be similar and
Oh, S. Y. +3 more
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Cyanide detoxification by recombinant bacterial rhodanese
Chemosphere, 2006Cyanide is a major environmental pollutant of the chemical and metallurgical industries. Although extremely toxic, cyanide can enzymatically be converted to the less toxic thiocyanate by rhodaneses (thiosulfate:cyanide sulfurtransferases, EC 2.8.1.1). We engineered a genetic system to express high levels of recombinant Pseudomonas aeruginosa rhodanese (
CIPOLLONE R +3 more
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Chemical Modification of Rhodanese with Sulphite
Free Radical Research Communications, 1991The essential sulphydryl group of bovine liver rhodanese (thiosulphate: cyanide sulphurtrasferase, E.C. 2.8.1.1.) is modified by sulphite produced during the enzymatic reaction or added to the fully active enzyme. The enzyme treated with labelled reagent incorporates 1 equivalent of SO3(2-) and loses one -SH group with the formation of a S-sulphonate ...
BERNI R +3 more
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Ferredoxin activation by rhodanese
Phytochemistry, 1974Abstract Rhodanese was extracted from Brassica oleracea leaves and purified 150-fold. The enzyme was shown to have optimum activity at pH 8-8.5 and a temperature range of 50-55°; a Km of 0.4 mM at 30° for thiosulphate and cyanide. and mol. wt around 32000.
Umberto Tomati +2 more
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Soil Science Society of America Journal, 1976
Abstract The detection of rhodanese (enzyme catalyzes the formation of SCN ‐ from S 2 O 3 2‐ and CN ‐ ) in soils is reported, and a ...
M. A. Tabatabai, B. B. Singh
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Abstract The detection of rhodanese (enzyme catalyzes the formation of SCN ‐ from S 2 O 3 2‐ and CN ‐ ) in soils is reported, and a ...
M. A. Tabatabai, B. B. Singh
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Phytochemistry, 1972
Abstract Rhodanese activity was detected in a crude extract of tapioca ( Manihot utilissima ) leaves. Optimal activity was found at a high pH (10·2–11·0) and temperature (57–59°). Under these conditions, rhodanese from 0·5 ml of the crude extract (75 mg leaf fr. wt.) catalysed the formation of 10·2 μmoles thiocyanate per 15 min.
M.Y. Chew, C.G. Boey
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Abstract Rhodanese activity was detected in a crude extract of tapioca ( Manihot utilissima ) leaves. Optimal activity was found at a high pH (10·2–11·0) and temperature (57–59°). Under these conditions, rhodanese from 0·5 ml of the crude extract (75 mg leaf fr. wt.) catalysed the formation of 10·2 μmoles thiocyanate per 15 min.
M.Y. Chew, C.G. Boey
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Nano-intercalated rhodanese in cyanide antagonism
Nanotoxicology, 2010Present studies have focused on nano-intercalated rhodanese in combination with sulfur donors to prevent cyanide lethality in a prophylactic mice model for future development of an effective cyanide antidotal system. Our approach is based on the idea of converting cyanide to the less toxic thiocyanate before it reaches the target organs by utilizing ...
Ilona, Petrikovics +7 more
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