Title : Lipoprotein lipase hydrolysis of trioleoylglycerol in a phospholipid interface. Effect of cholesteryl oleate on catalysis.

Pub. Date : 1985 Aug 15

PMID : 4019488






7 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Lipoprotein lipase hydrolysis of trioleoylglycerol in a phospholipid interface. Triolein lipoprotein lipase Bos taurus
2 The effect of cholesteryl oleate on the lipoprotein lipase-catalyzed hydrolysis of trioleoylglycerol was determined in monolayers of egg phosphatidylcholine at a constant surface pressure of 24 mN m-1. Triolein lipoprotein lipase Bos taurus
3 The initial rates of trioleoylglycerol hydrolysis were determined with lipoprotein lipase purified from bovine milk. Triolein lipoprotein lipase Bos taurus
4 Based on force-area measurements, the cholesteryl ester-mediated decrease in lipoprotein lipase activity observed at high substrate concentrations may be explained by displacement of trioleoylglycerol from the interface, thereby reducing the interfacial trioleoylglycerol concentration available for enzyme catalysis. Triolein lipoprotein lipase Bos taurus
5 Based on force-area measurements, the cholesteryl ester-mediated decrease in lipoprotein lipase activity observed at high substrate concentrations may be explained by displacement of trioleoylglycerol from the interface, thereby reducing the interfacial trioleoylglycerol concentration available for enzyme catalysis. Triolein lipoprotein lipase Bos taurus
6 One explanation for the cholesteryl oleate-mediated enhancement of lipoprotein lipase activity at low trioleoylglycerol concentrations is that the additional spreading of cholesteryl oleate disrupts microemulsions of trioleoylglycerol, thereby increasing the effective monomer substrate concentration available for enzyme catalysis. Triolein lipoprotein lipase Bos taurus
7 One explanation for the cholesteryl oleate-mediated enhancement of lipoprotein lipase activity at low trioleoylglycerol concentrations is that the additional spreading of cholesteryl oleate disrupts microemulsions of trioleoylglycerol, thereby increasing the effective monomer substrate concentration available for enzyme catalysis. Triolein lipoprotein lipase Bos taurus