Linked Life Data

12223468

Source:http://linkedlifedata.com/resource/pubmed/id/12223468

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
46
pubmed:dateCreated
2002-11-11
pubmed:abstractText
Phospholipase A(2) (PLA(2)) was purified to homogeneity from the supernatant fraction of rat testis homogenate. The purified 63-kDa enzyme did not require Ca(2+) ions for activity and exhibited both phosphatidic acid-preferring PLA(2) and monoacylglycerol lipase activities with a modest specificity toward unsaturated acyl chains. Anionic detergents enhanced these activities. Serine-modifying irreversible inhibitors, (p-amidinophenyl) methanesulfonyl fluoride and methylarachidonyl fluorophosphonate, inhibited both activities to a similar extent, indicating a single active site is involved in PLA(2) and lipase activities. The sequence of NH(2)-terminal 12 amino acids of purified enzyme was identical to that of a carboxylesterase from rat liver. The optimal pH for PLA(2) activity (around 5.5) differed from that for lipase activity (around 8.0). At pH 5.5 the enzyme also hydrolyzed bis(monoacylglycerol) phosphate, or lysobisphosphatidic acid (LBPA), that has been hitherto known as a secretory PLA(2)-resistant phospholipid and a late endosome marker. LBPA-enriched fractions were prepared from liver lysosome fractions of chloroquine-treated rats, treated with excess of pancreatic PLA(2), and then used for assaying LBPA-hydrolyzing activity. LBPA and the reaction products were identified by microbore normal phase high performance liquid chromatography/electrospray ionization ion-trap mass spectrometry. These enzymatic properties suggest that the enzyme can metabolize phosphatidic and lysobisphosphatidic acids in cellular acidic compartments.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
43674-81
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:12223468-Acyltransferases, pubmed-meshheading:12223468-Animals, pubmed-meshheading:12223468-Catalysis, pubmed-meshheading:12223468-Chloroquine, pubmed-meshheading:12223468-Chromatography, High Pressure Liquid, pubmed-meshheading:12223468-Esterases, pubmed-meshheading:12223468-Glycerides, pubmed-meshheading:12223468-Hydrogen-Ion Concentration, pubmed-meshheading:12223468-Hydrolysis, pubmed-meshheading:12223468-Lipid Metabolism, pubmed-meshheading:12223468-Liver, pubmed-meshheading:12223468-Lysophospholipids, pubmed-meshheading:12223468-Male, pubmed-meshheading:12223468-Mass Spectrometry, pubmed-meshheading:12223468-Monoglycerides, pubmed-meshheading:12223468-Pancreas, pubmed-meshheading:12223468-Phospholipases A, pubmed-meshheading:12223468-Phospholipases A2, pubmed-meshheading:12223468-Protein Structure, Tertiary, pubmed-meshheading:12223468-Rats, pubmed-meshheading:12223468-Rats, Sprague-Dawley, pubmed-meshheading:12223468-Substrate Specificity, pubmed-meshheading:12223468-Testis
pubmed:year
2002
pubmed:articleTitle
Purification and properties of a phospholipase A2/lipase preferring phosphatidic acid, bis(monoacylglycerol) phosphate, and monoacylglycerol from rat testis.
pubmed:affiliation
Department of Molecular Physiological Chemistry (H-1), Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't