Characterization of human placental blood vessel phospholipase a 2, demonstration of substrate selectivity for arachidonyl-phosphatidylcholine

1. 1. The hydrolysis of acyl esters in phosphatidylcholine by phospholipase A 2 (PLA 2) for human placental blood vessel was investigated. 2. 2. The enzyme displayed an alkaline pH optimum and an absolute requirement of Ca 2+ for activity. 3. 3. In contrast to rat tissues, the human placental blood...

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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 Elsevier B.V 1985
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Summary:1. 1. The hydrolysis of acyl esters in phosphatidylcholine by phospholipase A 2 (PLA 2) for human placental blood vessel was investigated. 2. 2. The enzyme displayed an alkaline pH optimum and an absolute requirement of Ca 2+ for activity. 3. 3. In contrast to rat tissues, the human placental blood vessel PLA 2 showed a selective preference for arachidonate over linoleate acyl group at the sn-2 position of phosphatidylcholine.
ISSN:0020-711X
DOI:10.1016/0020-711X(85)90054-0