Alpha-Glutamyl-beta-naphthylamide hydrolase of rabbit small intestine. Localization in the brush border and separation from other brush border peptidases.
About 70% of the total mucosal enzymatic activity hydrolyzing beta-L-glutamyl-beta-naphthylamide in the rabbit small intestine is present in the brush border; the specific activity in this subcellular fraction is 7 times higher than that of the homogenate. Similar results are obtained for L-leucyl beta-naphthylamide hydrolase. The enzyme activity is efficiently solubilized by papain digestion and is clearly separated from L-leucyl-beta-naphthylamide hydrolase by chromatography on concanavalin A-Sepharose. It probably represents a digestive peptidase, different from the other known peptide hydrolases of the digestive surface of the small intestine.
D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D005971:Glutamates; D006902:Hydroxymercuribenzoates / Q000494:pharmacology; D007413:Intestinal Mucosa / Q000201:enzymology*; D007421:Intestine, Small / Q000201:enzymology*; D007931:Leucyl Aminopeptidase / Q000378:metabolism; D008297:Male; D010206:Papain; D011691:Puromycin / Q000494:pharmacology; D011817:Rabbits; D012995:Solubility; D013329:Structure-Activity Relationship; D013347:Subcellular Fractions / Q000201:enzymology
D005971:Glutamates; D006902:Hydroxymercuribenzoates; D011691:Puromycin; D000626:Aminopeptidases; D007931:Leucyl Aminopeptidase; D010206:Papain