Linked Life Data

1359887

Source:http://linkedlifedata.com/resource/pubmed/id/1359887

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-12-4
pubmed:abstractText
We have purified two enzymic activities from flaxseed acetone powder: a lipoxygenase and a hydroperoxide dehydrase. The lipoxygenase activity belongs to an iron-containing protein having a molecular weight of 130 kDa which, upon incubation with alpha-linolenic acid, forms 13-hydroperoxy-9(Z), 11(E), 15(Z)- octadecatrienoic acid. The hydroperoxide dehydrase (a 55 kDa protein) metabolizes this hydroperoxide to an allene oxide which in turn is spontaneously hydrolyzed to alpha- and gamma-ketols. Relationships between these two enzymes were studied and results suggest an inhibition of the lipoxygenase by hydroperoxide dehydrase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
188
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
858-64
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Purification of lipoxygenase and hydroperoxide dehydrase in flaxseeds: interaction between these enzymatic activities.
pubmed:affiliation
U.R.A. C.N.R.S. 1485, Faculté de Médecine, Limoges, France.
pubmed:publicationType
Journal Article