Subunit structured of pig small-intestinal brush-border aminopeptidase N
نویسندگان
چکیده
منابع مشابه
Obligate Function of Brush Border Aminopeptidase
up peptide nutrients of two or three amino acid residues, but the mechanism of intestinal assimilation of larger oligopeptides has not been established. The amino-oligopeptidase of the intestinal brush border possesses high specificity for oligopeptides having bulky side chains and is a candidate for a crucial role in the overall assimilation of dietary protein. Rat jejunum was used for in vitr...
متن کاملShaping the intestinal brush border
Epithelial cells from diverse tissues, including the enterocytes that line the intestinal tract, remodel their apical surface during differentiation to form a brush border: an array of actin-supported membrane protrusions known as microvilli that increases the functional capacity of the tissue. Although our understanding of how epithelial cells assemble, stabilize, and organize apical microvill...
متن کاملRat Intestinal Brush Border Membrane Peptidases
The properties of two purified peptidases derived from the intestinal brush border membrane of the rat have been investigated. The pH optima, heat stabilities, substrate specificities, and metal ion requirements of the two enzymes and the effects of inhibitors on their activities were nearly identical. The isoenzymes catalyzed the hydrolysis of a wide range of peptides containing from 2 to 8 am...
متن کاملRelationship between peptide hydrolases in brush-border and cytosol fractions of guinea-pig intestinal mucosa.
Studies on the terminal stages of mammalian protein digestion, which is thought to involve the hydrolysis of peptides containing from two to six amino acids (Crampton et al., 1971), have been hampered by the fact that the enzymes involved appear to be distributed between two fractions of the mucosal cells (enterocytes), the brushborder and cytosol fractions (Peters, 1970). Some controversy exis...
متن کاملSimilarities between a dipeptide hydrolase from brush-border and cytosol fractions of guinea-pig intestinal mucosa.
A dipeptide hydrolase from the brush border of guinea-pig intestinal mucosa was purified. The enzyme resembles another dipeptide hydrolase isolated from the cytosol fraction of intestinal mucosa. Studies on the binding of cytosol peptide hydrolase to brush-border membranes indicate that the enzyme found in the brush border may be a cytoplasmic contaminant.
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1981
ISSN: 0264-6021
DOI: 10.1042/bj1970573