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Human gastric lipase. A kinetic study with dicaprin monolayers
Y Gargouri1, G Pieroni, F Ferrato
1Centre de Biochimie et de Biologie Moléculaire, CNRS, Marseille, France.
European Journal of Biochemistry
|November 16, 1987
Summary
Proteins like bovine serum albumin inhibit human gastric lipase activity by penetrating the lipid interface. This inhibition is not linked to interfacial tension or protein isoelectric points.
Area of Science:
- Biochemistry
- Enzymology
- Lipid Metabolism
Background:
- Human gastric lipase (HGL) is a key enzyme in dietary fat digestion.
- Understanding factors affecting HGL activity is crucial for digestive physiology.
- Protein interactions at lipid interfaces can modulate enzyme function.
Purpose of the Study:
- To investigate the inhibitory effects of various proteins on HGL.
- To determine the relationship between protein properties and HGL inhibition.
- To explore the mechanism of protein-induced HGL inhibition.
Main Methods:
- Assay of didecanoylglycerol hydrolysis by HGL at pH 3.0.
- Testing six different proteins: bovine serum albumin, myoglobin, soya bean lipase inhibitor, melittin, beta-lactoglobulin, and ovalbumin.
- Analysis of interfacial tension, isoelectric points, and protein penetration into lipid monolayers.
Main Results:
- Bovine serum albumin, myoglobin, and soya bean lipase inhibitor significantly inhibited HGL activity.
- Inhibition was not correlated with decreased interfacial tension or protein isoelectric points.
- Protein inhibition capacity correlated with their penetration power into the lipid interface.
Conclusions:
- Specific proteins can inhibit human gastric lipase activity.
- Protein penetration into the lipid interface is a key factor in HGL inhibition.
- HGL may exhibit greater penetration power than pancreatic lipase, despite higher susceptibility to interfacial denaturation.