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Article: The hydrolysis of phosphatidylcholine by phospholipase A2 in hamster heart

TitleThe hydrolysis of phosphatidylcholine by phospholipase A2 in hamster heart
Authors
Issue Date1984
Citation
Canadian Journal Of Biochemistry And Cell Biology, 1984, v. 62 n. 12, p. 1269-1274 How to Cite?
AbstractThe hydrolysis of acyl esters in phosphatidylcholine and phosphatidylethanolamine by phospholipase A in hamster heart subcellular fractions was investigated. Phosphatidylcholine was found to be a much poorer substrate than phosphatidylethanolamine for the cardiac phospholipase A. The rate of hydrolysis of phosphatidylcholine by microsomal phospholipase A was 10-fold less than with phosphatidylethanolamine as substrate. When 1-[1-14C]palmitoyl-2-acyl phosphatidyl-[Me-3H]choline was used as substrate, both phospholipase A1 and A2 activities were detected in all subcellular fractions, but the highest specific activities for both enzymes were located in the microsomal fraction. However, phospholipase A2 activity in all hamster heart particulate fractions was three to six times higher than phospholipase A1 activity. The hydrolysis of phosphatidylcholine by microsomal phospholipase A2 displayed an alkaline pH optimum and an absolute requirement for Ca2+ or Mg2+. The enzyme also depicted high specificity towards polyunsaturated acyl groups at the C-2 position of phosphatidylcholine.
Persistent Identifierhttp://hdl.handle.net/10722/170748
ISSN
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorTam, SWen_US
dc.contributor.authorMan, RYKen_US
dc.contributor.authorChoy, PCen_US
dc.date.accessioned2012-10-30T06:10:41Z-
dc.date.available2012-10-30T06:10:41Z-
dc.date.issued1984en_US
dc.identifier.citationCanadian Journal Of Biochemistry And Cell Biology, 1984, v. 62 n. 12, p. 1269-1274en_US
dc.identifier.issn0714-7511en_US
dc.identifier.urihttp://hdl.handle.net/10722/170748-
dc.description.abstractThe hydrolysis of acyl esters in phosphatidylcholine and phosphatidylethanolamine by phospholipase A in hamster heart subcellular fractions was investigated. Phosphatidylcholine was found to be a much poorer substrate than phosphatidylethanolamine for the cardiac phospholipase A. The rate of hydrolysis of phosphatidylcholine by microsomal phospholipase A was 10-fold less than with phosphatidylethanolamine as substrate. When 1-[1-14C]palmitoyl-2-acyl phosphatidyl-[Me-3H]choline was used as substrate, both phospholipase A1 and A2 activities were detected in all subcellular fractions, but the highest specific activities for both enzymes were located in the microsomal fraction. However, phospholipase A2 activity in all hamster heart particulate fractions was three to six times higher than phospholipase A1 activity. The hydrolysis of phosphatidylcholine by microsomal phospholipase A2 displayed an alkaline pH optimum and an absolute requirement for Ca2+ or Mg2+. The enzyme also depicted high specificity towards polyunsaturated acyl groups at the C-2 position of phosphatidylcholine.en_US
dc.languageengen_US
dc.relation.ispartofCanadian Journal of Biochemistry and Cell Biologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshChemical Phenomenaen_US
dc.subject.meshChemistryen_US
dc.subject.meshCricetinaeen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshMesocricetusen_US
dc.subject.meshMyocardium - Enzymology - Metabolismen_US
dc.subject.meshPhosphatidylcholines - Metabolismen_US
dc.subject.meshPhosphatidylethanolaminesen_US
dc.subject.meshPhospholipases - Metabolismen_US
dc.subject.meshPhospholipases A - Metabolismen_US
dc.subject.meshPhospholipases A1en_US
dc.subject.meshPhospholipases A2en_US
dc.subject.meshSubcellular Fractions - Enzymologyen_US
dc.subject.meshSubstrate Specificityen_US
dc.titleThe hydrolysis of phosphatidylcholine by phospholipase A2 in hamster hearten_US
dc.typeArticleen_US
dc.identifier.emailMan, RYK:rykman@hkucc.hku.hken_US
dc.identifier.authorityMan, RYK=rp00236en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid6529700-
dc.identifier.scopuseid_2-s2.0-0021669103en_US
dc.identifier.volume62en_US
dc.identifier.issue12en_US
dc.identifier.spage1269en_US
dc.identifier.epage1274en_US
dc.identifier.isiWOS:A1984ACL0800001-
dc.identifier.scopusauthoridTam, SW=7202036985en_US
dc.identifier.scopusauthoridMan, RYK=7004986435en_US
dc.identifier.scopusauthoridChoy, PC=7006633002en_US

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