Linked Life Data

1103979

Source:http://linkedlifedata.com/resource/pubmed/id/1103979

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1976-2-26
pubmed:abstractText
A method was developed for the reassembly of membranous vesicle from the sodium deoxycholate-dissociated outer membrane components of Escherichia coli. The removal of the detergent by dialysis and the presence of Mg2+ were essential for the reassembly. Membrane protein alone did not form any membranous structure. Closed membranous vesicles similar to the native outer membrane were reassembled only when protein was mixed with both lipopolysaccharide and phospholipid in deoxycholate solution and subsequently dialized. The membrane showed a distinct trilaminar structure with a center-to-center distance between two dark lines of 53 A, which is a characteristic of the native outer membrane. This characteristic trilaminar structure was shown to be due to the presence of lipopolysaccharide. Phospholipd was required for the vesicularization of membrane. Lipopolysaccharide and/or phospholipid formed a membranous structure in the absence of protein, while the morphology of their negatively stained sample was quite different from that of the native outer membrane unless the outer membrane protein was added to the reassembly mixture. The protein from the cytoplasmic membrane was unable to reform membranous vesicle with lipopolysaccharide and phospholipid, indicating that the reassembly system discriminated outer membrane proteins from cytoplasmic proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
413
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
371-93
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
In vitro reassembly of the membranous vesicle from Escherichia coli outer membrane components. Role of individual components and magnesium ions in reassembly.
pubmed:publicationType
Journal Article