| Literature DB >> 1244859 |
G Andria, A Marzi, S Auricchio.
Abstract
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.Entities:
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Year: 1976 PMID: 1244859 DOI: 10.1016/0005-2736(76)90370-9
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002