Results 181 to 190 of about 6,015 (201)
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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.
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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.
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Selenium Binding to Beef‐Kidney Rhodanese
European Journal of Biochemistry, 1975The reaction of beef kidney rhodanese with selenosulfate was studied. The selenium‐treated enzyme shows an absorption spectrum with a maximum at 375 nm attributable to a sulfoselenide group. This absorption is bleached by addition of cyanide. After cyanide treatment stoichiometric amount of selenocyanate can be found.The intrinsic fluorescence of ...
C, Cannella +5 more
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Primary structure of avian hepatic rhodanese
Journal of Protein Chemistry, 1990Rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1.) was purified from chicken livers and its amino acid sequence was determined. The enzyme has a specific activity of 676 IU and a molecular weight of 32,255. The primary structure of 289 amino acids was solved by sequential Edman degradation of overlapping peptides obtained by selected ...
R A, Kohanski, R L, Heinrikson
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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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Rhodanese domain-containing sulfurtransferases
2019Sulfur is an essential element for the growth and development of plants, which synthesize cysteine and methionine from the reductive assimilation of sulfate. Besides its incorporation into proteins, cysteine is the building block for the biosynthesis of numerous sulfur-containing molecules and cofactors.
Selles, Benjamin +3 more
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The double domain structure of rhodanese
Journal of Molecular Biology, 1975A 3 A electron density map of bovine liver rhodanese shows, in conjunction with gel electrophoresis experiments, that rhodanese consists of a single polypeptide chain with molecular weight of 32,000. The map reveals a very clear double domain structure of the molecule. The two domains are of equal size and have very similar conformations.
Bergsma, J. +5 more
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Thiosulphate sulphurtransferase (rhodanese) in cephalopoda
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1981Abstract 1. 1. The distribution of rhodanese activity in the homogenate and hyaloplasm obtained from gills, digestive gland and kidney of four cephalopods has been studied. 2. 2. The enzyme activity, which seems to be ubiquitous, is much higher in the octopods ( Octopus vulgaris Lam.
Claudio Agnisola +4 more
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Properties of Azotobacter vinelandii rhodanese.
Biochemistry and molecular biology international, 1993Rhodanese (thiosulfate: cyanide sulfurtransferase, E.C. 2.8.1.1) was purified from the nitrogen fixing organism Azotobacter vinelandii, and its amino acid composition was determined. The enzyme is a single polypeptide chain of M(r) 29,000 which showed an apparent pI of 4.7 and no presence of isoenzymes.
S, Pagani +3 more
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Cyanide Detoxifying Enzyme: Rhodanese
Current Biotechnology e, 2012Mayank Chaudhary, Reena Gupta
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