Pancreatic Lipase Activity in Deuterium Oxide.

Abstract

Summary The activity of purified pancreatic lipase, with tributyrin emulsified in gum arabic as the substrate, has been studied in ordinary water and in varying concentrations of D₂O up to 100%. Estimates of maximum reaction velocities indicate that the degree of inhibition increases linearly with increasing D₂O. At low substrate concentrations, however, the inhibition produced by D₂O was much less, an indication that there is a stronger solvent effect on enzyme-substrate binding than on the rate of hydrolysis itself.