title: Role of a sulfhydryl group in gastric lipases. A binding study using the monomolecular-film technique.
abstract: Native human and rabbit gastric lipases (HGL and RGL, respectively) were inactivated after modification of one sulfhydryl group/enzyme molecule. HGL and RGL were covalently labeled using 5,5'-dithiobis(2-nitro-[14C]benzoic acid) and the interaction of 2-nitro-5-thio-[14C]benzoic-acid-labeled lipases ([14C]Nbs-lipases) with monomolecular lipid films was investigated. Our results show that [14C]Nbs-lipases bind to lipid films as efficiently as native HGL or RGL. The critical surface pressure pi c and the maximal surface pressure (delta pi max) of [14C]Nbs-lipases were enhanced in comparison with those of native RGL and HGL. These changes in behavior were probably due to an increase in hydrophobicity brought about, directly or indirectly, by the binding of the Nbs radical. This chemical modification thus blocks the hydrolysis site and reinforces the hydrophobic character of the gastric lipases.
authors.affiliation: Centre de Biochimie et de Biologie Moléculaire du Centre National de la Recherche Scientifique, Marseille, France.
authors.forename: Y
authors.initials: Y
authors.lastname: Gargouri
authors.forename: H
authors.initials: H
authors.lastname: Moreau
authors.forename: G
authors.initials: G
authors.lastname: Pieroni
authors.forename: R
authors.initials: R
authors.lastname: Verger
mesh_terms: D000818:Animals; D001665:Binding Sites; D002250:Carbon Radioisotopes; D004228:Dithionitrobenzoic Acid / Q000378:metabolism*; D005750:Gastric Juice / Q000201:enzymology; D006801:Humans; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D008066:Lipolysis; D009579:Nitrobenzoates / Q000378:metabolism*; D011312:Pressure; D011485:Protein Binding; D011817:Rabbits; D013438:Sulfhydryl Compounds / Q000378:metabolism; D013499:Surface Properties
chemical_list: D002250:Carbon Radioisotopes; D009579:Nitrobenzoates; D013438:Sulfhydryl Compounds; D004228:Dithionitrobenzoic Acid; D008049:Lipase