Results 91 to 100 of about 178 (132)
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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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Immunohistochemical localization of rhodanese
The Histochemical Journal, 1990The role of rhodanese in the detoxication of acute cyanide exposure is controversial. The debate involves questions of the availability of rhodanese to cyanide in the peripheral circulation. Blood-borne cyanide will distribute to the brain and may induce lesions or even death.
M, Sylvester, C, Sander
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Reaction of rhodanese with dithiothreitol
Biochimica et Biophysica Acta (BBA) - Enzymology, 1976The reaction between bovine rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1) and reduced dithiothreitol has been studied. This reagent, in the absence of thiosulfate, reduces the amount of sulfur carried by rhodanese with formation of sulfide and oxidized dithiothreitol: E-S-SH + reduced dithiothreitol replaced by E-SH + HS- + oxidized ...
L, Pecci +4 more
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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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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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The cystathionase-rhodanese system
Biochimica et Biophysica Acta (BBA) - Enzymology, 1967Abstract Cystathionase ( l -homoserine hydrolase (deaminating), EC 4.2.1.15) and rhodanese ∗∗ (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) have been combined to form a coupled enzyme system which is capable of utilizing cysteine sulfur for transsulfuration. The initial product of the action of Cystathionase on cystine, thiocysteine, is, at
T W, Szczepkowski, J L, Wood
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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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Recombinant bovine rhodanese: purification and comparison with bovine liver rhodanese
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992Recombinant bovine rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) has been purified to homogeneity from Escherichia coli BL21(DE3) by cation-exchange chromatography. Recombinant and bovine liver rhodanese coelectrophorese under denaturing conditions, with an apparent subunit molecular weight of 33,000.
D M, Miller +5 more
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Rhodanese isozymes in human tissues
Annals of Human Genetics, 1988SummaryAn investigation of a range of tissue homogenates by various electrophoretic methods, followed by staining for specific enzyme activity, has revealed a series of isozymes of human rhodanese. Polyacrylamide gel isoelectric focusing provided the most data and rhodanese activity was found in all of the tissues examined. The simplest isozyme pattern
D B, Whitehouse +3 more
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Thermodynamics of zinc binding to rhodanese
Archives of Biochemistry and Biophysics, 1974Abstract The binding of zinc ion (Zn2+) to rhodanese at two pH values was studied by microcalorimetry and the free energy, enthalpy, and entropy changes determined. Binding exhibited rather large endothermic enthalpy changes quite similar to those observed for zinc-model compound interactions.
D W, Bolen, S, Rajender
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