Open AccessHuman gastric lipase
Author(s) -
GARGOURI Youssef,
PIERONI Gérard,
FERRATO Francine,
VERGER Robert
Publication year - 1987
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1987.tb13588.x
Subject(s) - lipase , isoelectric point , chemistry , melittin , biochemistry , bovine serum albumin , myoglobin , hydrolysis , triacylglycerol lipase , enzyme , denaturation (fissile materials) , chromatography , peptide , nuclear chemistry
The effects of several proteins on the hydrolysis at pH 3.0 of didecanoylglycerol monolayers by human gastric lipase were investigated. Among the six proteins tested (bovine serum albumin, myoglobin, a protein inhibiting lipase isolated from soya bean, melittin, β‐lactoglobulin and ovalbumin), only the first three proteins were found to inhibit lipase activity. The inhibition capacity of the proteins was not related to the decrease in interfacial tension or to their isoelectric points. However, inhibition of human gastric lipase by proteins may be correlated with the penetration power of the protein into the lipid interface. It is hypothesized that this lipase has a higher penetration power than that of pancreatic lipase, even though the former enzyme is more susceptible to interfacial denaturation.