Linked Life Data

8243462

Source:http://linkedlifedata.com/resource/pubmed/id/8243462

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-12-30
pubmed:abstractText
When arachidonate 12-lipoxygenase purified from porcine leukocytes was incubated aerobically with 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine, the phospholipid reacted at up to 30% of the rate of a free fatty acid substrate; the esterified arachidonic acid was oxygenated predominantly to the (12S)-12-hydroperoxy product. The porcine leukocyte enzyme was also capable of metabolizing phosphatidylcholine containing esterified (15S)-15-hydroperoxy-5,8,11,13-eicosatetraenoic acid; oxygenation occurred predominantly at the 14R position. Reaction with mitochondrial and endoplasmic membranes of rat liver produced esterified (12S)-12-hydroperoxy-5,8,10,14-eicosatetraenoic acid and (13S)-13-hydroperoxy-9,11-octadecadienoic acid as major oxygenation products. Thus, porcine leukocyte 12-lipoxygenase is capable of oxygenating not only free polyenoic fatty acids but also more complex substrates such as phospholipids and biomembranes. In contrast, the human platelet 12-lipoxygenase is almost inactive with these esterified polyenoic fatty acids. In regard to the function of these enzymes, the leukocyte-type of 12-lipoxygenase has similar catalytic activities to the mammalian 15-lipoxygenase and its physiological function may include the structural modification of membrane lipids.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
218
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
165-71
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Investigation of the oxygenation of phospholipids by the porcine leukocyte and human platelet arachidonate 12-lipoxygenases.
pubmed:affiliation
Department of Biochemistry, Tokushima University School of Medicine, Japan.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't