THE SPECIFICITY OF AN INTESTINAL LIPASE FOR MONOGLYCERIDES

Abstract

An enzyme found in the homogenates of rat intestinal mucosa has been demonstrated to be specific for the hydrolysis of 1- and 2-monoglycerides. During a two hour incubation at 37 C, both 1- and 2-monoglycerides are hydrolyzed to a comparable extent (17-19%). Under the same conditions, diand triglycerides undergo little or no hydrolysis. This enzyme appears to be different from most enzymes previously reported in the intestinal mucosa or succus entericus. The enzymes previously reported have their major activity directed toward the hydrolysis of triglycerides only or hydrolyze mono-, di-, and triglycerides at approximately equal rates. The exact role of this monoglyceride specific lipase is difficult to delineate. Since pancreatic lipase is specific for the hydrolysis of the 1- and 3-positions of triglycerides, this enzyme may have a definite role in the completion of normal digestion of triglycerides. (Author)

Document Details

Document Type
Technical Report
Publication Date
May 09, 1961
Accession Number
AD0255749

Entities

People

  • James C. Mcpherson
  • William W. Jr. Burr

Organizations

  • University of Texas at Austin

Tags

DTIC Thesaurus Topics

  • Biomolecules
  • Chemical Compounds
  • Digestive System Processes
  • Glycerides
  • Hydrolysis
  • Incubation
  • Lipids

Fields of Study

  • Biology

Readers

  • Analytical Chemistry
  • Immunology