| Autor: |
Ransac S; Centre de Biochimie et de Biologie Moléculaire, C.N.R.S., Marseille, France., Deveer AM, Rivière C, Slotboom AJ, Gancet C, Verger R, De Haas GH |
| Jazyk: |
angličtina |
| Zdroj: |
Biochimica et biophysica acta [Biochim Biophys Acta] 1992 Jan 03; Vol. 1123 (1), pp. 92-100. |
| DOI: |
10.1016/0005-2760(92)90175-u |
| Abstrakt: |
For the first time, we have shown that a stereospecific interaction occurs between porcine pancreatic phospholipase A2 and a monomolecular film of amidophospholipid used as inhibitor. Direct binding experiments, using radiolabelled phospholipase A2, showed that 13 times more enzyme was bound to phospholipid films of the L series by comparison with films of the D series. These results were confirmed by indirect binding studies using re-spreading experiments. Kinetic studies of the porcine pancreatic PLA2, using enantiomeric acyl-amino phospholipid analogues, have shown that: (1) inhibitors of the L series are more potent than inhibitors of the D series, (2) inhibitors having a negative charge are more potent than zwitterionic inhibitors, (3) inhibitory power values are greater when evaluated in micellar system than in a the monolayer system, (4) the inhibitory power increases continuously with surface pressure. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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