Linked Life Data

7044896

Source:http://linkedlifedata.com/resource/pubmed/id/7044896

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
1982-8-26
pubmed:abstractText
Ovalbumin is secreted by the tubular gland cells without cleavage of a signal sequence at the N-terminus. In Escherichia coli strains which produce a chicken ovalbumin-like protein (OLP) from a plasmid-cloned gene, the OLP is synthesized on membrane-bound polysomes and secreted without cleavage into the periplasmic space. In contrast, a deleted protein, which lacks 126 amino acids in the N-terminal half, is not secreted and is synthesized from free polysomes. Our results are compatible with the presence, in the N-terminal half of the molecule, of a signal sequence necessary for the transport across the membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
79-87
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Secretion into the bacterial periplasmic space of chicken ovalbumin synthesized in Escherichia coli.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't