R1756
Rhodanese from bovine liver
Type II, essentially salt-free, lyophilized powder, 100-300 units/mg solid
Synonym(s):
Thiosulfate Sulfur Transferase, Thiosulfate:cyanide sulfurtransferase
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About This Item
CAS Number:
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.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
低风险生物材料
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Sabria Mimoun et al.
Antioxidants & redox signaling, 17(1), 1-10 (2012-03-01)
Sulfide is released in the large intestine lumen by the microbiota and is an inhibitor of mitochondrial respiration and a genotoxic agent in colonocytes when present in excess. Deciphering how colonocytes metabolize sulfide is an important issue. In this study
Liming Luo et al.
Plant molecular biology, 79(4-5), 495-508 (2012-05-31)
Rhodanese-domain proteins (RDPs) are widespread in plants and other organisms, but their biological roles are mostly unknown. Here we report on a novel RDP from Chlamydomonas that has a single rhodanese domain, and a predicted chloroplast transit peptide. The protein
Dan Su et al.
FEBS letters, 586(6), 717-721 (2012-02-02)
5-Methylaminomethyl-2-selenouridine (mnm(5)Se(2)U) is found in the first position of the anticodon in certain tRNAs from bacteria, archaea and eukaryotes. This selenonucleoside is formed in Escherichia coli from the corresponding thionucleoside mnm(5)S(2)U by the monomeric enzyme YbbB. This nucleoside is present
Assylay Kurmanbayeva et al.
Methods in molecular biology (Clifton, N.J.), 1631, 253-271 (2017-07-25)
In response to oxidative stress the biosynthesis of the ROS scavenger, glutathione is induced. This requires the induction of the sulfate reduction pathway for an adequate supply of cysteine, the precursor for glutathione. Cysteine also acts as the sulfur donor
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
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