Interfacial structure and lipase action. Characterization of taurodeoxycholate-didecanoylglycerol monolayers by physical and kinetic methods.
Surface pressure-area isotherms for 1,3-didecanoyl-glycerol (dicaprin) were determined as a function of the concentration of taurodeoxycholate in the subphase. Analysis of these curves indicates that, from 0.05 to 0.80 mM bile salt, surface structure is dependent only on the surface concentration of the diglyceride. The limiting areas for dicaprin in the presence and absence of bile salt were about 38 A2/molecule. Subjecting the monolayers to hydrolysis by pancreatic lipase yielded kinetic data which, together with the physical studies, support a model for monolayer glyceride molecules undergoing discrete changes of state. In the absence of bile salt, the relatively expanded state exhibits an area of 75 A2/diglyceride molecule and is not a substrate for pancreatic lipase B. The more condensed state exhibits an area of 38 A2/diglyceride molecule and is hydrolyzed at a rate proportional to its concentration in the monolayer. Taurodeoxybholate at 0.05 to 0.60 mM shifts the apparent area of the expanded state to 360 A2/diglyceride molecule.
D000818:Animals; D003089:Colipases; D003840:Deoxycholic Acid / Q000031:analogs & derivatives; D004075:Diglycerides; D005989:Glycerides; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D008567:Membranes, Artificial; D008958:Models, Molecular; D008968:Molecular Conformation; D010179:Pancreas / Q000201:enzymology; D011312:Pressure; D013499:Surface Properties; D013552:Swine; D013657:Taurodeoxycholic Acid; D013816:Thermodynamics
D003089:Colipases; D004075:Diglycerides; D005989:Glycerides; D008567:Membranes, Artificial; D003840:Deoxycholic Acid; D013657:Taurodeoxycholic Acid; D008049:Lipase