Linked Life Data

3046946

Source:http://linkedlifedata.com/resource/pubmed/id/3046946

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-10-24
pubmed:abstractText
Immunoblotting of size-separated whole cell proteins permitted the study of protein-protein interaction. Briefly, proteins obtained from cleared cell lysates of Escherichia coli were separated by glycerol gradient centrifugation and analysed by blotting against a set of specific antibodies. We have applied this procedure to the assembly of 11 N-terminal amber fragments of the beta subunit of E. coli RNA polymerase ranging in size between 97% and 23% the length of the intact beta polypeptide (1342 amino acids). In this way, we have been able to define regions on the beta polypeptide involved in the assembly of RNA polymerase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
176
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
403-7
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Assembly of amber fragments of the beta subunit of Escherichia coli RNA polymerase.
pubmed:affiliation
Department of Biochemistry, Queen's Medical Centre, Nottingham, England.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't