Results 81 to 90 of about 178 (132)
On the Active Group in Rhodanese. [PDF]
Bo H. Sörbo +5 more
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Reversible folding of rhodanese
S Tandon, P M Horowitz
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Mechanism of Rhodanese Action: Polarographic Studies
J R, GREEN, J, WESTLEY
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PROBING THE ACTIVE SITE OF RHODANESE WITH DISULFIDE REAGENTS [PDF]
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Journal of Chemical Ecology, 1985
Forty-four species of insects were assayed for the presence of rhodanese, an enzyme generally considered to be responsible for the detoxification of cyanide. Rhodanese was found to be widely distributed in both adults and larvae and was not restricted to those species which encounter exogenous cyanide through feeding on cyanogenic plants. These results
Jones David A
exaly +3 more sources
Forty-four species of insects were assayed for the presence of rhodanese, an enzyme generally considered to be responsible for the detoxification of cyanide. Rhodanese was found to be widely distributed in both adults and larvae and was not restricted to those species which encounter exogenous cyanide through feeding on cyanogenic plants. These results
Jones David A
exaly +3 more sources
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 ...
Rodolfo Berni +2 more
exaly +4 more sources
Is there rhodanese activity in plants?
Phytochemistry, 1992Abstract In view of the possible role of rhodanese in the HCN detoxification of cyanogenic plants, a method to measure low rhodanese levels is proposed. As the spontaneous formation of thiocyanate can mimic low levels of rhodanese activity, the influence of the composition of the reaction mixture on the spontaneous thiocyanate formation was studied ...
P Kakes
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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
exaly +2 more sources
Determination of rhodanese in plants
Phytochemistry, 1990Abstract The standard rhodanese test used for extracts from animal tissues does not work in plant homogenates due to the concomitant occurrence of both enzymatic and non-enzymatic thiocyanate production. Rhodanese activity is generally determined by the enzymatic formation of SCN − from thiosulphate and cyanide.
Dirk SELMAR, Reinhard Lieberei
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Phytochemistry, 1973
Abstract Rhodanese activity was detected in crude leaf extracts of 12 randomly selected plant species consisting of 9 non-cyanophoric and 3 cyanophoric species. In each case, the enzyme exhibited high activity at pH 10·4 and 55°. There appeared to be no correlation between rhodanese activity and the cyanophoric nature of the plant.
exaly +2 more sources
Abstract Rhodanese activity was detected in crude leaf extracts of 12 randomly selected plant species consisting of 9 non-cyanophoric and 3 cyanophoric species. In each case, the enzyme exhibited high activity at pH 10·4 and 55°. There appeared to be no correlation between rhodanese activity and the cyanophoric nature of the plant.
exaly +2 more sources

