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Encapsulation of thiosulfate: Cyanide sulfurtransferase by mouse erythrocytes
Toxicology and Applied Pharmacology, 1986Murine carrier erythrocytes, prepared by hypotonic dialysis, were employed in the encapsulation of several compounds including [14C]sucrose, [3H]inulin, and bovine thiosulfate:cyanide sulfurtransferase (rhodanese), a mitochondrial enzyme which converts cyanide to thiocyanate.
P, Leung +5 more
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Clinical Biochemistry, 2009 To test the hypothesis that impaired expression of the thiosulfate sulfurtransferase rhodanese is associated with oxidative stress and may predict mortality in hemodialysis patients.Sixty-two hemodialysis patients were investigated to determine protein and mRNA expression of rhodanese in monocytes.
Katharina Krueger +4 more
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Purification of thiosulfate sulfurtransferase by selective immobilization on blue agarose
Analytical Biochemistry, 1978 Abstract A new method for isolating crystalline bovine liver thiosulfate sulfurtransferase has been developed which relies on the selective binding of the enzyme to agarose-immobilized Cibacron Blue F3GA. This preparation has the advantages of simplicity, reproducibility, and rapidity.
Paul M. Horowitz
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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982 The active-site sulfhydryl group in the enzyme thiosulfate sulfurtransferase (rhodanese; thiosulfate:cyanide sulfurtransferase; EC 2.8.1.1) is alkylated rapidly by iodoacetic acid in the free enzyme form, E, with complete loss of sulfurtransferase activity.
Paul M. Horowitz, Nick L. Criscimagna
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Nitric Oxide, 2014 Background Increased H2S availability reduces injury associated with myocardial ischemia (MI) and ischemia–reperfusion. The mitochondrial enzyme thiosulfate sulfurtransferase (TST) has a putative role in removal of H2S and is a potential target to increase H2S bioavailability.
Barry Emerson +4 more
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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982 Structural transitions occurring in the range of 0-50 degrees C have been detected and studied in the enzyme thiosulfate sulfurtransferase (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1) by investigating both the intrinsic protein fluorescence and the fluorescence of covalently bound probes.
Zygmunt Wasylewski, Paul M. Horowitz
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Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1987
Rhodanese levels have been measured in liver, kidney and plasma from a number of species. Liver activity was low in marmosets, pigeons and beagle bitches. Levels were high in rats and somewhat lower in hamsters and guinea pigs while levels in two strains of rabbits were intermediate between guinea pigs and marmosets.
R B, Drawbaugh, T C, Marrs
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Rhodanese levels have been measured in liver, kidney and plasma from a number of species. Liver activity was low in marmosets, pigeons and beagle bitches. Levels were high in rats and somewhat lower in hamsters and guinea pigs while levels in two strains of rabbits were intermediate between guinea pigs and marmosets.
R B, Drawbaugh, T C, Marrs
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Journal of biochemical and molecular toxicology, 2014
We assessed the dose-dependent effect of potassium cyanide (KCN) on thiosulfate sulfurtransferase (TST), 3-mercaptopyruvate sulfurtransferase (3-MPST), and cystathionine λ-lyase (CST) activities in mice. The time-dependent effect of 0.5 LD50 KCN on cyanide level and cytochrome c oxidase (CCO), TST, 3-MPST, and CST activities was also examined ...
Poonam, Singh +2 more
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We assessed the dose-dependent effect of potassium cyanide (KCN) on thiosulfate sulfurtransferase (TST), 3-mercaptopyruvate sulfurtransferase (3-MPST), and cystathionine λ-lyase (CST) activities in mice. The time-dependent effect of 0.5 LD50 KCN on cyanide level and cytochrome c oxidase (CCO), TST, 3-MPST, and CST activities was also examined ...
Poonam, Singh +2 more
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Thiosulfate Sulfurtransferase Deficiency Promotes Oxidative Distress in Cerebral Prefrontal Cortex
Free Radical Biology and Medicine, 2023Yang Luo +7 more
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