Linked Life Data

11254178

Source:http://linkedlifedata.com/resource/pubmed/id/11254178

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-3-19
pubmed:abstractText
Cyanide detoxification is catalysed by two enzymes: rhodanese [thiosulphate: cyanide sulphurtransferase, E.C. 2.8.1.1], and 3-mercaptopyruvate sulphurtransferase [3-MST, EC. 2.8.1.2]. In the present work, the activity of the two enzymes in the crude extracts of different tissues and in the mitochondrial and cytosolic fractions of tissues from some ruminants (camels, cattle and sheep) and birds (chickens and pigeons) have been compared. Rhodanese activity was almost exclusively present in the mitochondrial fraction. In ruminants and chickens the highest activity of rhodanese was found in the liver, followed by the kidney. In pigeons, however, the enzyme activity was the highest in the kidneys. In camels' tissues, the rhodanese activity was significantly (P < 0.05) lower than in cattle or sheep, and the enzyme activities in the two latter species were similar. The activity of 3-MST in the crude extract of tissues from camels was similar to that in sheep, but higher than that in cattle. The enzyme activity was equally distributed between the mitochondrial and cytosolic fractions in the liver and kidneys of camels, cattle and sheep.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0928-4249
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
63-70
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Tissue and intracellular distribution of rhodanese and mercaptopyruvate sulphurtransferase in ruminants and birds.
pubmed:affiliation
Department of Veterinary Medicine, College of Agriculture and Veterinary Medicine, King Saud University, Buraydah, Saudi Arabia. alibadreldin@hotmail.com
pubmed:publicationType
Journal Article