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An enzyme present in the microsomes of small intestinal mucosa cells was partially purified by a combination of several conventional methods: solubilization with deoxycholate, (NH4)2SO4 fractionation, diethylaminoethyl Sephadex column chromatography, carboxymethyl Sephadex treatment, and finally starch zone electrophoresis. The purified enzyme preparation had a specific activity 300 times that of the starting homogenate. The enzyme showed little if any hydrolytic activity on long chain di- and triglycerides, cholesterol esters, lecithin, and acetylcholine. It hydrolyzed all medium and long chain monoglycerides tested, except monostearin, and a variety of short chain esters including mono-, and di-, triglycerides as well as methyl and ethyl esters. The substrate specificity pattern indicates that this enzyme acts on soluble substrates and might be considered an esterase proper rather than a lipase. However, since this enzyme has been previously referred to as monoglyceride lipase together with the fact that the most probable physiological substrates are long chain monoglycerides, this designation might be preferable.
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Pope et al. (1966) studied this question.
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