Linked Life Data

7042181

Source:http://linkedlifedata.com/resource/pubmed/id/7042181

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1982-7-22
pubmed:abstractText
1. Hydrolysis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid (PABA-peptide) has been measured in soluble and particulate fractions of human small intestinal mucosa. 2. Both soluble and particulate fractions contained enzymic activity capable of splitting the PABA-peptide. In the particulate fractions this activity increased threefold towards the distal small intestine. 3. Neither soluble nor particulate activity was inhibited by the chymotrypsin inhibitor 1-chloro-4-phenyl-3-L-toluene-p-sulphonamidobutan-2-one (TPCK). 4. Column chromatography on Sephacryl S-300 resolved a peak of PABA-peptide hydrolase activity that was clearly distinct from other known brush-border peptide hydrolases and from added chymotrypsin standard. 5. This PABA-peptide hydrolase thus represents a distinct intestinal enzyme, possibly bound to the brush-border membrane, which could account for the residual urinary PABA recovery observed in patients and animal models with exocrine pancreatic insufficiency.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0143-5221
pubmed:author
pubmed:issnType
Print
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
557-60
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Non-pancreatic hydrolysis of N-benzoyl-l-tyrosyl-p-aminobenzoic acid (PABA-peptide) in the human small intestine.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't