QUANTIFICATION OF THE INTERACTION OF LYSOLECITHIN WITH PHOSPHATIDYLCHOLINE VESICLES USING BOVINE SERUM-ALBUMIN - RELEVANCE TO THE ACTIVATION OF PHOSPHOLIPASE-A(2)

The activity of soluble phospholipase A2 to hydrolyze phosphatidylcholine vesicles increases abruptly after a lag time of several minutes. The onset of this apparent activation event probably results from the accumulation of a threshold mole fraction of the hydrolysis products (lysolecithin and fatty acid) in the bilayer. One important observation relevant to the mechanism of this activation process is the biphasic dependence of the lag time on vesicle concentration. To test whether this dependence can be attributed entirely to the strength of partitioning of the lysolecithin into the phosphatidylcholine bilayer, we estimated the apparent partition coefficient of lysophospholipid in the membrane of phosphatidylcholine vesicles. Based on competition between bovine serum albumin and the vesicles for the lysophospholipid, we estimated the partition coefficient to be about 5 . 10(-7) or palmitoyl lipids at 39-degrees-C and about 9 . 10(-7) for myristoyl lipids at 22-degrees-C. These values were able to rationalize the behavior of the lag time with dipalmitoylphosphatidylcholine vesicles, but they were unable to predict the behavior with dimyristoylphosphatidylcholine. Therefore, it appears that the complete dependence of the lag phase on vesicle concentration must be explained by additional means such as the possible contribution of nascent fatty acid or previously proposed kinetic activation mechanisms.