A lipase was found to be present in dog stomach which appeared to be more abundant in the fundic than in the pyloric mucosa. Dog gastric lipase was extracted by soaking the gastric tissue and further purified after cation exchange, anion exchange and gel-filtration using fast protein liquid chromatography. The amino-acid composition, N-terminal amino-acid sequence, substrate specificity, interfacial and kinetic behavior and inactivation by sulfhydryl reagents were determined and compared with those of human and rabbit gastric lipases. We report for the first time that a gastric lipase is 13 times more active on long-chain than on short-chain triacylglycerols at pH 4.0, reaching a maximal specific activity of 950 U/mg on Intralipide emulsion.As early as 1901, Volhard showed that human gastric juice could hydrolyze triacylglycerols and concluded that the stomach was an important site of fat digestion containing a lipase which was named human gastric lipase [l]. Although several authors have since then confirmed the existence of preduodenal lipolysis in many other species, there is still some debate as to the tissular and cellular location as well as the exact physiological role of preduodenal lipases in mammals.It has by now been clearly established that preduodenal lipases can hydrolyze long-chain triacylglycerols and their physiological importance was probably under-estimated in the past. Even patients suffering from pancreatic insufficiency have an appreciable fat intake, probably because the low pancreatic lipase activity is compensated for by a strong gastric lipase activity [2 -51.
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