Differential hydrolysis of 1-alkyl-2-acyl and diacylglycerophosphocholines by human and non-human phospholipases A2.
The activity of two human phospholipases A2, purified from synovial fluid and lumbar disc herniations, was tested using alkylacyl- and diacylglycerophosphocholines and the influence of the chemical link at the sn-1 position of glycerol was investigated. Both enzymes exhibited 2.5-3-fold selectivity for 1-ester-linked compared to 1-ether-linked phosphatidylcholine. No significant selectivity was observed with pancreatic phospholipase A2 while Naja naja naja venom enzyme was more efficient against 1-ether-phospholipids.
Cabré
F
F
R & D Department, Laboratorios Menarini S.A., Badalona, Spain.
García
A M
AM
Carabaza
A
A
Mauleón
D
D
Carganico
G
G
D004546:Elapid Venoms / Q000201:enzymology*; D006801:Humans; D006868:Hydrolysis; D010179:Pancreas / Q000201:enzymology; D010713:Phosphatidylcholines / Q000378:metabolism*; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2; D010972:Platelet Activating Factor / Q000031:analogs & derivatives* / Q000378:metabolism
C036761:1-alkyl-2-acyl-sn-glycero-3-phosphocholine; D004546:Elapid Venoms; D010713:Phosphatidylcholines; D010972:Platelet Activating Factor; D010741:Phospholipases A; D054467:Phospholipases A2