Zymogram studies of human intestinal brush border and cytoplasmic peptidases.
Zymogram studies of peptide hydrolases from the human intestinal brush border and cytoplasmic fractions produced multiple bands--that is, up to seven--while the brush border membrane produced only a single band of enzyme activity. With all of the substrates tested except L-leucyl-L-leucyl-L-leucine, a band having anodic mobility identical with that produced by the brush border enzymes was produced by the cytoplasmic enzymes. With L-trileucine as a substrate, no overlapping band was produced. This band in the cytoplasmic fraction was heat sensitive, while that in the brush border fraction was not. Thus it would appear that there is a single human intestinal brush border peptide hydrolase capable of hydrolysing a variety of di- and tri-peptides. This peptide hydrolases of the brush border and the cytoplasmic fraction of human intestine are distinct.
D002462:Cell Membrane / Q000201:enzymology*; D003593:Cytoplasm / Q000201:enzymology; D004151:Dipeptides; D004586:Electrophoresis; D006358:Hot Temperature; D006801:Humans; D007413:Intestinal Mucosa / Q000201:enzymology*; D008871:Microvilli / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D010455:Peptides
D004151:Dipeptides; D010455:Peptides; D010447:Peptide Hydrolases