Results 161 to 170 of about 6,015 (201)

Tannic acid inhibits TNF-α signaling by targeting the protein disulfide isomerase and alleviates symptoms in an imiquimod-induced psoriasis mouse model. [PDF]

open access: yesCell Commun Signal
Jin W   +16 more
europepmc   +1 more source

Deep-sea corals near cold seeps associate with sulfur-oxidizing chemoautotrophs in the family Ca. Thioglobaceae. [PDF]

open access: yesMicrobiome
Vohsen SA   +7 more
europepmc   +1 more source

Rhodanese in insects

Journal of Chemical Ecology, 1985
Forty-four species of insects were assayed for the presence of rhodanese, an enzyme generally considered to be responsible for the detoxification of cyanide. Rhodanese was found to be widely distributed in both adults and larvae and was not restricted to those species which encounter exogenous cyanide through feeding on cyanogenic plants. These results
S G, Beesley, S G, Compton, D A, Jones
openaire   +2 more sources

Immunohistochemical localization of rhodanese

The Histochemical Journal, 1990
The role of rhodanese in the detoxication of acute cyanide exposure is controversial. The debate involves questions of the availability of rhodanese to cyanide in the peripheral circulation. Blood-borne cyanide will distribute to the brain and may induce lesions or even death.
M, Sylvester, C, Sander
openaire   +2 more sources

The cystathionase-rhodanese system

Biochimica et Biophysica Acta (BBA) - Enzymology, 1967
Abstract Cystathionase ( l -homoserine hydrolase (deaminating), EC 4.2.1.15) and rhodanese ∗∗ (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) have been combined to form a coupled enzyme system which is capable of utilizing cysteine sulfur for transsulfuration. The initial product of the action of Cystathionase on cystine, thiocysteine, is, at
T W, Szczepkowski, J L, Wood
openaire   +2 more sources

Recombinant bovine rhodanese: purification and comparison with bovine liver rhodanese

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992
Recombinant bovine rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) has been purified to homogeneity from Escherichia coli BL21(DE3) by cation-exchange chromatography. Recombinant and bovine liver rhodanese coelectrophorese under denaturing conditions, with an apparent subunit molecular weight of 33,000.
D M, Miller   +5 more
openaire   +2 more sources

Reaction of rhodanese with dithiothreitol

Biochimica et Biophysica Acta (BBA) - Enzymology, 1976
The reaction between bovine rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1) and reduced dithiothreitol has been studied. This reagent, in the absence of thiosulfate, reduces the amount of sulfur carried by rhodanese with formation of sulfide and oxidized dithiothreitol: E-S-SH + reduced dithiothreitol replaced by E-SH + HS- + oxidized ...
L, Pecci   +4 more
openaire   +2 more sources

Rhodanese isozymes in human tissues

Annals of Human Genetics, 1988
SummaryAn investigation of a range of tissue homogenates by various electrophoretic methods, followed by staining for specific enzyme activity, has revealed a series of isozymes of human rhodanese. Polyacrylamide gel isoelectric focusing provided the most data and rhodanese activity was found in all of the tissues examined. The simplest isozyme pattern
D B, Whitehouse   +3 more
openaire   +2 more sources

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