Results 151 to 160 of about 3,211 (192)
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Interspecies differences in rhodanese (thiosulfate sulfurtransferase, EC 2.8.1.1) activity in liver, kidney and plasma

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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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.
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The specificity of active-site alkylation by iodoacetic acid in the enzyme thiosulfate sulfurtransferase

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.
P, Horowitz, N L, Criscimagna
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A Fluorescence study of conformational changes induced by substrate and temperature in bovine liver thiosulfate sulfurtransferase

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.
Z, Wasylewski, P M, Horowitz
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P4 Myocardial ischaemic injury is unexpectedly increased in mice lacking the H2S metabolising enzyme thiosulfate sulfurtransferase

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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221 Myocardial Ischemic Injury Is Unexpectedly Increased In Mice Lacking The H2s Metabolising Enzyme Thiosulfate Sulfurtransferase

Heart, 2014
Background Increased H2S availability, through use of H2S donors, or in mice overexpressing the H2S synthetic enzyme cystathionine gamma-lyase (CSE), reduces injury associated with myocardial ischemia (MI) and ischemia-reperfusion.
Barry Emerson   +4 more
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Thiosulfate sulfurtransferase

2023
Silvia Buonvino   +2 more
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Dose and time-dependent effects of cyanide on thiosulfate sulfurtransferase, 3-mercaptopyruvate sulfurtransferase, and cystathionine λ-lyase activities.

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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Integrative oncology: Addressing the global challenges of cancer prevention and treatment

Ca-A Cancer Journal for Clinicians, 2022
Jun J Mao,, Msce   +2 more
exaly  

Thiosulfate Sulfurtransferase Deficiency Promotes Oxidative Distress in Cerebral Prefrontal Cortex

Free Radical Biology and Medicine, 2023
Yang Luo   +7 more
openaire   +1 more source

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