Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1985-6-19
pubmed:abstractText
Human beta-endorphin was digested by neutral metalloendopeptidase from rabbit kidney and the products were isolated and identified. Based on the structure and yield of the fragments, the major cleavage sites were identified with the Leu17-Phe18, Gly3-Phe4, Pro13-Leu14 and Ile22-Ile23 peptide bonds of the beta-endorphin structure. The cleavage of the Leu17-Phe18 bond appears to be the rate-limiting step of the enzymic conversion similarly to the previously proposed pathways of beta-endorphin degradation by brain homogenates and synaptic membranes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0143-4179
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13-9
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Action of neutral metalloendopeptidase ("enkephalinase") on beta-endorphin.
pubmed:publicationType
Journal Article