Abstract
The peptidases located in the intestinal brush border (BB) probably play a major role in the pathophysiology of protein digestion, but their properties are still incompletely known. In the present study, rabbit BB activities hydrolyzing Phe-Ala(PA), Leu-Gly-Gly (LGG) and Leu-B-naphthylamide (LNA) showed high specific activities and amounted to about 20%, 13% and 5O%, respectively, of the total mucosal activity for the same substrate. PA hydrolase of the BB differed from that of the cytosol on the basis of the following data…(mean±SEM):
Ion exchange chromatography separated the BB peptidases, after solubilization with papain, in 3 peaks. The main peak was active towards dipeptides (PA, Gly-Leu, Lys-Leu), tripeptides (LGG, Phe3) and arylamides (LNA, Lys-NA), whereas a 2nd one hydrolyzed dipeptides, with no LNAase and very low tripeptidase activity. PA hydrolases of both peaks were phHB and heat insensitive and only that of the 1st peak was inhibited (about 50%) by puromycin. The 3rd peak contained the γ -Gln-NAase activity.
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Andria, G., Marzi, A. & Auricchio, S. PEPTIDASE ACTIVITIES OF THE BRUSH BORDER OF RABBIT SMALL INTESTINAL MUCOSA. Pediatr Res 8, 141 (1974). https://doi.org/10.1203/00006450-197402000-00093
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DOI: https://doi.org/10.1203/00006450-197402000-00093