R1756
Rhodanese from bovine liver
Type II, essentially salt-free, lyophilized powder, 100-300 units/mg solid
别名:
Thiosulfate Sulfur Transferase, Thiosulfate:cyanide sulfurtransferase
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关于此项目
化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
100-300 units/mg solid
type
Type II
form
essentially salt-free, lyophilized powder
specific activity
100-300 units/mg solid
storage temp.
−20°C
Quality Level
Application
Rhodanese (RHOD) is an enzyme that converts cyanide to thiocyanate. RHOD may be useful in ulcerative colitis (UC) research as it has been shown to have detoxifying properties in the colon . Rhodanese is used to study sulfur energy metabolism .
Biochem/physiol Actions
Rhodanese (RHOD) is the principal enzyme involved in hydrogen sulphide (H2S) detoxication in the colonic luman .
Other Notes
One unit will convert 1.0 μmole of cyanide to thiocyanate per min at pH 8.6 at 25°C.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
低风险生物材料
此项目有
Tomohiro Mizobata et al.
PloS one, 6(10), e26462-e26462 (2011-10-27)
The Escherichia coli chaperonin GroEL subunit consists of three domains linked via two hinge regions, and each domain is responsible for a specific role in the functional mechanism. Here, we have used circular permutation to study the structural and functional
Piotr Sura et al.
Comparative biochemistry and physiology. Toxicology & pharmacology : CBP, 154(3), 180-186 (2011-05-25)
The effect of mercury ions on the level of cysteine, glutathione, sulfane sulfur, and on the activity of rhodanese, 3-mercaptopyruvate sulfurtransferase (MPST) and γ-cystathionase in brain, heart muscle, liver, kidneys, testes and skeletal muscle of adult Xenopus laevis was investigated.
Hossein Tayefi-Nasrabadi et al.
TheScientificWorldJournal, 2012, 648085-648085 (2012-05-26)
Cyanide is one of the most toxic substances present in a wide variety of food materials that are consumed by animals. Rhodanese, a ubiquitous enzyme, can catalyse the detoxification of cyanide by sulphuration reaction. In this study, rhodanese was partially
Yoshihiro Sasaki et al.
Macromolecular bioscience, 11(6), 814-820 (2011-03-09)
Cell-free protein synthesis is a promising technique for the rapid production of proteins. However, the application of the cell-free systems requires the development of an artificial chaperone that prevents aggregation of the protein and supports its correct folding. Here, nanogel-based
Girish C Melkani et al.
Bioscience reports, 32(3), 299-303 (2012-01-26)
The chaperonin GroEL binds to non-native substrate proteins via hydrophobic interactions, preventing their aggregation, which is minimized at low temperatures. In the present study, we investigated the refolding of urea-denatured rhodanese at low temperatures, in the presence of ox-GroEL (oxidized
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