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Journal of Lipid Research, Vol. 9, 79-84, January 1968
Copyright © 1968 by Lipid Research, Inc.
The Procter & Gamble Company, Miami Valley Laboratories, Cincinnati, Ohio 45239
The relative rates of hydrolysis of the secondary ester in glycerol 1,3-benzylidene 2-oleate and in glycerol 1,3-dihexadecyl ether 2-oleate, and of the primary and secondary esters in triolein were determined. Both unaltered and selectively inactivated rat pancreatic juice were used as sources of enzyme. It was found that rat pancreatic juice contains an enzyme that can hydrolyze fatty acids esterified at the 2-position of a glyceride. This enzyme is not pancreatic lipase. It may be sterol ester hydrolase. Partial glycerides, as well as complete glycerides, can serve as substrates. Pancreatic lipase, if it can hydrolyze the 2-positioned fatty acids of a triglyceride, does so at a very slow rate.
Supplementary key words enzyme specificity digestion absorption pancreatic lipase cholesterol esterase structure of triglycerides
Submitted on August 10, 1967
Accepted on September 20, 1967
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