Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1994-8-8
pubmed:abstractText
The activity was studied of enkephalinase (endopeptidase 24.11, neutral endopeptidase)--a membrane enzyme of epithelial cells within human digestive tract (in the stomach, duodenum, small intestine, ascending, descending and sigmoid colon, and rectum). The enzyme activity was determined by column method using the labelled substrate (H-D-AlaLeu)--enkephalin and the selective enkephalin inhibitor--thiorfan in the presence of bestatin and captopril--inhibitors of aminopeptidases and angiotensin converting enzyme respectively. The highest enkephalinase activity was found in the duodenal epithelium (77.3 8.0 fmol of the substrate/min/mg of protein) and in the small intestine (23.4 0.9 fmol/min/mg of protein) with its gradual decrease when progressing down the gastrointestinal tract. This result confirms the hypothesis of enkephalinase participation in protein hydrolysis processes.
pubmed:language
pol
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0043-5147
pubmed:author
pubmed:issnType
Print
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
[Activity of enkephalinase (EC.3.4.24.11). Neutral endopeptidase (NEP)in human digestive tract epithelial cells].
pubmed:affiliation
Kliniki Gastroenterologii Ak. Med., Lublinie.
pubmed:publicationType
Journal Article, English Abstract