SOD1 Is an Integral Yet Insufficient Oxidizer of Hydrogen Sulfide in Trisomy 21 B Lymphocytes and Can Be Augmented by a Pleiotropic Carbon Nanozyme. [PDF]
Mouli K+7 more
europepmc +1 more source
Alteration of Gene Expression After Entecavir and Pegylated Interferon Therapy in HBV-Infected Chimeric Mouse Liver. [PDF]
Bao H+11 more
europepmc +1 more source
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 ...
Pooja Rao+2 more
exaly +4 more sources
Is Thiosulfate Sulfurtransferase the Colonic Sulfide Oxidase?
Neither sodium sulfide nor sodium thiosulfate is soluble in ethanol but NaHS.H20 is. We then removed insoluble material from our preparations by centrifugation and discarded it. The ethanol-soluble material was used in the experiments. In this later study we were able to show that removal of thiosulfate sulfurtransferase (TST), using a specific ...
Margaret C. Eggo+4 more
openaire +3 more sources
Some comparisons between solution and crystal properties of thiosulfate sulfurtransferase
The activity and crystal stability of the enzyme thiosulfate sulfurtransferase were studied as a function of ionic strength. At 2 M ammonium sulfate, where the x-ray structural studies of this protein were done soluble enzyme has low activity (
Paul M. Horowitz, Kuldeep Patel
openaire +4 more sources
Purification of thiosulfate sulfurtransferase by selective immobilization on blue agarose
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
openaire +4 more sources
[37] Thiosulfate: Cyanide sulfurtransferase (Rhodanese)
Publisher Summary This chapter presents a procedure for the preparation of cyanide sulfurtransferase, which was discovered as the result of a search for the active principle in the tissues of animals known to be able to convert cyanide to the less toxic thiocyanate. The thiocyanate product is determined calorimetrically as its red complex with Fe(III)
John Westley
openaire +4 more sources
Thiosulfate sulfurtransferase (rhodanese) in forest soils
Concentrations of thiosulfate sulfurtransferase (rhodanese; EC 2.8.1.1) in soils of five types of forest stands (spruce and pine stands without ground vegetation, and mountain ash, birch and pine stands with grass cover) were followed. Soils from grassed stands contained much higher concentrations of the enzyme than soils without ground vegetation.
A. Lettl
openaire +3 more sources
221 Myocardial Ischemic Injury Is Unexpectedly Increased In Mice Lacking The H2s Metabolising Enzyme Thiosulfate Sulfurtransferase [PDF]
Background Increased H 2 S availability, through use of H 2 S donors, or in mice overexpressing the H 2 S synthetic enzyme cystathionine gamma-lyase (CSE), reduces injury associated with myocardial ischemia (MI) and ischemia-reperfusion. The mitochondrial enzyme thiosulfate sulfurtransferase (TST) has a putative role in removal of H 2 S and inhibition
Gillian A. Gray+4 more
openaire +3 more sources
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.
Paul M. Horowitz, Zygmunt Wasylewski
openaire +4 more sources