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
应用
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 .
生化/生理作用
Rhodanese (RHOD) is the principal enzyme involved in hydrogen sulphide (H2S) detoxication in the colonic luman .
其他说明
One unit will convert 1.0 μmole of cyanide to thiocyanate per min at pH 8.6 at 25°C.
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
低风险生物材料
此项目有
Rui Qiu et al.
Protein and peptide letters, 19(11), 1139-1143 (2012-05-17)
Yeast tRNA-thiouridine modification protein 1 (Tum1) plays essential role in the sulfur transfer process of Urm1 system, which in turn is involved in many important cellular processes. In the rhodanese-like domain (RLD), conserved cysteine residue is proved to be the
Vicky De Preter et al.
Inflammatory bowel diseases, 18(12), 2371-2380 (2012-03-22)
Defective detoxification of sulfides leads to damage to the mucosa and may play a role in the etiology of ulcerative colitis (UC). The colonic mucosal thiosulfate sulfurtransferase (TST) enzyme removes H(2) S by conversion to the less toxic thiocyanate. In
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
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
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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