| Autor: |
Burke JR; Drug Discovery Research, Bristol-Myers Squibb Pharmaceutical Research Institute, Buffalo, New York, 14213, USA., Witmer MR, Tredup JA |
| Jazyk: |
angličtina |
| Zdroj: |
Archives of biochemistry and biophysics [Arch Biochem Biophys] 1999 May 15; Vol. 365 (2), pp. 239-47. |
| DOI: |
10.1006/abbi.1999.1151 |
| Abstrakt: |
Cytosolic phospholipase A2 (cPLA2) is normally located in the cytosol, but in response to cellular activation the enzyme binds to the membrane at the lipid/water interface where it catalyzes the hydrolysis of the sn-2 ester of arachidonate-containing phospholipids. Synthetic phospholipid vesicle systems have been used in kinetic and mechanistic analyses of cPLA2, but these systems result in a rapid loss of enzyme activity. In the present research, covesicles of 1,2-dimyristoyl-sn-glycero-3-phosphomethanol (DMPM) containing (Copyright 1999 Academic Press.) |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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