Linked Life Data

1404244

Source:http://linkedlifedata.com/resource/pubmed/id/1404244

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-10-30
pubmed:abstractText
The enzyme mercaptopyruvate sulfurtransferase appears to play an important role in the in vivo detoxification of cyanide. It does so by transferring sulfur to cyanide to produce thiocyanate, which is less toxic and may be excreted through the kidney. Several compounds were tested for their ability to affect the rate of enzyme catalyzed thiocyanate formation in vitro. The studies were carried out using both a partially purified bovine kidney extract and a highly purified enzyme preparation. Hypotaurine and methanesulfinic acid doubled sulfurtransferase activity in the partially purified extract at 30 mM, but inhibited the purified enzyme to 57% (hypotaurine) and 27% (methanesulfinic acid) of control activity at the same concentration. Pyruvate, phenylpyruvate, oxobutyrate, and oxoglutarate each inhibited the extract and purified forms of mercaptopyruvate sulfurtransferase. Phenylpyruvate was the most effective inhibitor, reducing activity to 0.2% of control values in the extract, and 11% of control values for purified MPST when added to the reaction at 30 mM. Other compounds tested (see Table 1) had a negligible effect on sulfurtransferase activity. A heat stable cofactor was found in boiled kidney extract which stimulated sulfurtransferase activity in the extract but inhibited sulfurtransferase activity in the purified enzyme, as was observed for hypotaurine and methanesulfinate. The boiled extract had no thiocyanate forming activity of its own. The cofactor operated in synergy with methanesulfinate, but independently of hypotaurine.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/3-mercaptopyruvate..., http://linkedlifedata.com/resource/pubmed/chemical/3-mercaptopyruvic acid, http://linkedlifedata.com/resource/pubmed/chemical/Cyanides, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine, http://linkedlifedata.com/resource/pubmed/chemical/Phenylpyruvic Acids, http://linkedlifedata.com/resource/pubmed/chemical/Pyruvates, http://linkedlifedata.com/resource/pubmed/chemical/Sulfinic Acids, http://linkedlifedata.com/resource/pubmed/chemical/Sulfurtransferases, http://linkedlifedata.com/resource/pubmed/chemical/Taurine, http://linkedlifedata.com/resource/pubmed/chemical/Thiocyanates, http://linkedlifedata.com/resource/pubmed/chemical/Tissue Extracts, http://linkedlifedata.com/resource/pubmed/chemical/hypotaurine, http://linkedlifedata.com/resource/pubmed/chemical/methanesulfinic acid, http://linkedlifedata.com/resource/pubmed/chemical/phenylpyruvic acid
pubmed:status
MEDLINE
pubmed:issn
0887-2082
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
65-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Modifiers of mercaptopyruvate sulfurtransferase catalyzed conversion of cyanide to thiocyanate in vitro.
pubmed:affiliation
Pharmacology Division, US Army Medical Research Institute of Chemical Defense, Aberdeen Proving Ground, MD 21010.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't