Abstract
A new method for the assay of peptidase activities is developed based on the oxidative deamination of L-amino acids with L-amino acid oxidase. This method measures the products of the enzymatic hydrolysis, without any interfrence from the peptides.
Brush border membrane hydrolvzes very rapidly tri- and tetra-L-alanine, L-lencyl-glycyl glycine, L-leucyl-glycine, L-phenylalanyl-L-alanine, and L-leucine amide.
The enzymatic activities of the brush border membrane hydrolyzing L-phenylalayl-L-alanine and L-leucine amide were characterized with regard to pH-activity curves, ion activation, and intracellular distribution.
The results suggest that intrinsic enzymes of the brush border membrane play a role in the teminal digestion of proteins.
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Auricchio, S., Pifrro, M. & Orsatil, M. 9. Peptidase activities of brush border membrane of rat intestine. Pediatr Res 5, 84 (1971). https://doi.org/10.1203/00006450-197102000-00014
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DOI: https://doi.org/10.1203/00006450-197102000-00014