Linked Life Data

1881386

Source:http://linkedlifedata.com/resource/pubmed/id/1881386

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-9-27
pubmed:abstractText
The selective distribution of methionyl aminopeptidase (MAP) among rat liver mitochondria (heavy and light) and microsomes is reported. Several properties of MAP from the three subcellular fractions showed that the enzyme is a typical aminopeptidase able to remove N-terminal methionine from oligopeptides and methionyl-2-naphthylamide but not from Met-Ala-Ser. MAP is a membrane-bound enzyme sensitive to SH-group oxidants and inhibitable by L-methionine but not by usual arylaminopeptidase inhibitors. It is suggested that, MAP may play an important role during protein synthesis in rat liver.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
102
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
101-13
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Methionyl aminopeptidase from rat liver: distribution of the membrane-bound subcellular enzyme.
pubmed:affiliation
Department of Biochemistry, Universidade Federal do Rio Grande do Sul, Porto Alegre, Brazil.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't