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R1756

Sigma-Aldrich

Rhodanese from bovine liver

Type II, essentially salt-free, lyophilized powder, 100-300 units/mg solid

Sinónimos:

Thiosulfate Sulfur Transferase, Thiosulfate:cyanide sulfurtransferase

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About This Item

Número de CAS:
9026-04-4
Comisión internacional de enzimas:
2.8.1.1 (BRENDA, IUBMB)
MDL number:
MFCD00132178
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type II

Quality Level

200

form

essentially salt-free, lyophilized powder

specific activity

100-300 units/mg solid

storage temp.

−20°C

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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 .

Unit Definition

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_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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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
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
Avinash Kale et al.
The Journal of biological chemistry, 286(24), 21254-21265 (2011-04-29)
The PEB4 protein is an antigenic virulence factor implicated in host cell adhesion, invasion, and colonization in the food-borne pathogen Campylobacter jejuni. peb4 mutants have defects in outer membrane protein assembly and PEB4 is thought to act as a periplasmic
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