Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1982-6-14
pubmed:abstractText
We show, using a simple, rapid fractionation method, that the precursor to the filamentous phage major coat protein is an integral membrane protein. The method, which consists of treatment of Escherichia coli with 0.1 N NaOH followed by centrifugation, leaves a subset of inner and outer membrane proteins in the NaOH pellet. Most proteins partition into the NaOH pellet (membrane) or supernatant (cytoplasm and periplasm) in a manner consistent with their subcellular location as determined by more conventional techniques. We find no evidence for cytoplasmic filamentous phage pre-coat protein in either wild-type of mutant-infected cells. Our evidence suggests that a protein identified as "soluble procoat" by K. Ito, G. Mandell and W. Wickner may be the amber fragment of a different phage protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
177-84
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Filamentous phage pre-coat is an integral membrane protein: analysis by a new method of membrane preparation.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.