Phospholipase activity of bovine milk lipoprotein lipase on phospholipid vesicles: influence of apolipoproteins C-II and C-III. |
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Authors: | H G Muntz N Matsuoka R L Jackson |
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Institution: | 1. Department of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine Cincinnati, Ohio 45267 USA;2. Department of Biological Chemistry University of Cincinnati College of Medicine Cincinnati, Ohio 45267 USA;3. Department of Medicine University of Cincinnati College of Medicine Cincinnati, Ohio 45267 USA |
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Abstract: | The effect of human plasma apolipoproteins C-II and C-III on the hydrolytic activity of lipoprotein lipase from bovine milk was determined using dimyristoyl phosphatidylcholine (DMPC) vesicles as substrate. In the absence of apoC-II or C-III, lipoprotein lipase has limited phospholipase activity. When the vesicles were preincubated with apoC-II and then phospholipase activity determined, there was a time dependent release of lysolecithin; activity was dependent upon both apoC-II and lipoprotein lipase concentrations. The addition of apoC-III to DMPC did not stimulate phospholipase activity. We conclude that apoC-II has an activator effect on the phospholipase activity of lipoprotein lipase and that the mechanism is beyond that of simply altering the lateral compressibility of the lipid. |
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