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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Reciprocal effect of apolipoprotein C-II on the lipoprotein lipase-catalyzed hydrolysis of p-nitrophenyl butyrate and trioleoylglycerol.

Interaction of purified bovine milk lipoprotein lipase ( LpL) with sonicated vesicles of dipalmitoyl phosphatidylcholine in the gel phase is associated with an increase in the rate of the LpL-catalyzed hydrolysis of p-nitrophenyl butyrate. There is a 6-fold increase in Vmax. Apolipoprotein C-II, the activator protein for LpL, inhibits the LpL-catalyzed hydrolysis of p-nitrophenyl butyrate. With 0.5 mol % tri[14C]oleoylglycerol present in the dipalmitoyl phosphatidylcholine vesicles and in the presence of 20 mM Ca2+, the rate of p-nitrophenyl butyrate hydrolysis is decreased reciprocally compared to trioleoylglycerol hydrolysis and is dependent on apolipoprotein C-II. These results suggest that apolipoprotein C-II enhances the activity of LpL by increasing the affinity of the active site of LpL for triacylglycerol.[1]

References

  1. Reciprocal effect of apolipoprotein C-II on the lipoprotein lipase-catalyzed hydrolysis of p-nitrophenyl butyrate and trioleoylglycerol. Shirai, K., Jackson, R.L., Quinn, D.M. J. Biol. Chem. (1982) [Pubmed]
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