Characterization of human placental blood vessel phospholipase A2, demonstration of substrate selectivity for arachidonyl-phosphatidylcholine

The hydrolysis of acyl esters in phosphatidylcholine by phospholipase A2 (PLA2) for human placental blood vessel was investigated. The enzyme displayed an alkaline pH optimum and an absolute requirement of Ca2+ for activity. In contrast to rat tissues, the human placental blood vessel PLA2 showed a...

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Published inInternational journal of biochemistry Vol. 17; no. 12; pp. 1317 - 1319
Main Authors Karnauchow, T M, Chan, A C
Format Journal Article
LanguageEnglish
Published England 1985
Subjects
Arachidonic Acids - metabolism
Blood Vessels - cytology
Blood Vessels - enzymology
Calcium - pharmacology
Female
Humans
Hydrogen-Ion Concentration
Phosphatidylcholines - metabolism
Phospholipases - isolation & purification
Phospholipases A - isolation & purification
Phospholipases A2
Phospholipid Ethers
Placenta - blood supply
Pregnancy
Substrate Specificity
Time Factors
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Summary:The hydrolysis of acyl esters in phosphatidylcholine by phospholipase A2 (PLA2) for human placental blood vessel was investigated. The enzyme displayed an alkaline pH optimum and an absolute requirement of Ca2+ for activity. In contrast to rat tissues, the human placental blood vessel PLA2 showed a selective preference for arachidonate over linoleate acyl group at the sn-2 position of phosphatidylcholine.
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SourceType-Scholarly Journals-1
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ISSN:0020-711X
DOI:10.1016/0020-711X(85)90054-0