Linked Life Data

6993477

Source:http://linkedlifedata.com/resource/pubmed/id/6993477

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1980-9-23
pubmed:abstractText
Cell-free arabinose binding protein (ABP) was synthesized using a mRNA-directed Escherichia coli S30 translation system. The source of the mRNA was a total cellular RNA extract from cultures of E. coli B/r ara A 39, induced for ABP production. Purification of in vitro ABP was effected by affinity chromatography on a column of purified anti-ABP coupled to Sepharose 4B, followed by Sephadex G-75 chromatography in 9% formic acid. The purified in vitro ABP was found to have a molecular weight approximately 3000 greater than native ABP. Comparison of the CNBr peptide fragments of native and in vitro ABP demonstrated an NH2-terminal extension of 23 amino acids not present in native ABP. The identities of 20 of the residues in the extension were established, and the characteristics of this region resemble the features proposed for signal sequences that function in protein secretion.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
255
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6745-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
The NH2-terminal sequence of a precursor form of the arabinose binding protein.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.