Results 111 to 120 of about 1,815 (145)

Thiosulfate sulfurtransferase

open access: closed, 2023
Silvia Buonvino   +2 more
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P13 Cardiovascular phenotyping in mice with thiosulfate sulfurtransferase gene knock-out

open access: closedNitric Oxide, 2013
Background Hydrogen sulfide (H2S) is increasingly recognised as a key cardiovascular mediator with effects on the heart and vasculature in health and disease [1] , [2] . H2S is generated endogenously via cystathionine gamma-lyase (CSE) and cystathionine beta-synthase (CBS), whilst bioavailability can also be increased by H2S donors.
Barry Emerson   +3 more
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Some comparisons between solution and crystal properties of thiosulfate sulfurtransferase

open access: closedBiochemical and Biophysical Research Communications, 1980
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
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Thiosulfate-thiol sulfurtransferase

open access: closed, 1997
Dietmar Schomburg, Dörte Stephan
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Is Thiosulfate Sulfurtransferase the Colonic Sulfide Oxidase?

open access: closedDigestive Diseases and Sciences, 2007
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
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Thiosulfate sulfurtransferase (rhodanese) in forest soils

open access: closedFolia Microbiologica, 1987
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
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On the molecular weight of thiosulfate sulfurtransferase

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975
Bovine liver thiosulfate sulfurtransferase (rhodanese) (EC 2.8.1.1) HAS BEEN REPORTED TO EXIST IN SOLUTION IN A RAPID, PH-dependent equilibrium between monomeric and dimeric forms of molecular weights 18 500 and 37 000 (Volini, M., DeToma, F. and Westley, J. (1967), J. Biol. Chem. 242, 5220).
L M, Ellis, C K, Woodward
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