Linked Life Data

2373079

Source:http://linkedlifedata.com/resource/pubmed/id/2373079

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-8-24
pubmed:abstractText
Based on the liberation of proline from ProLeuGlyNH2 (MIF-1, melanostatin) manganese-activated prolyl aminopeptidase activities were purified from rat brain and kidney cytosolic fractions. They were distinguished from other di- and tripeptidases and an arylamidase liberating N-terminal proline. Purified prolyl aminopeptidase from both sources had identical molecular properties (native Mr 300,000, subunit Mr 54,000) and very similar catalytic properties. The action of the purified enzymes was not restricted to proline. Other, in particular lipophilic, amino acids were cleaved from di-, tri- and oligopeptides with even higher velocities. Peptides with N-terminal penultimate proline residues were not degraded. From a comparison of molecular data, action on peptides, influence of pH values, inhibitors and activators, it is concluded that the activity is identical with leucyl aminopeptidase (EC 3.4.11.1) and that a separate prolyl aminopeptidase (EC 3.4.11.5) does not exist in rats.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
190
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
509-15
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Prolyl aminopeptidase from rat brain and kidney. Action on peptides and identification as leucyl aminopeptidase.
pubmed:affiliation
Anatomisches Institut, Universität Kiel, Federal Republic of Germany.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't