Linked Life Data

1369484

Source:http://linkedlifedata.com/resource/pubmed/id/1369484

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1992-8-14
pubmed:abstractText
Overexpression of the asnA gene from Escherichia coli K-12 coding for asparagine synthetase (EC 6.3.1.1) was achieved with a plasmid, pUNAd37, a derivative of pUC18, in E. coli. The plasmid was constructed by optimizing a DNA sequence between the promoter and the ribosome binding region. The enzyme, comprising ca. 15% of the total soluble protein in the E. coli cell, was readily purified to apparent homogeneity by DEAE-Cellulofine and Blue-Cellulofine column chromatographies. The amino-terminal sequence, amino acid composition, and molecular weight of the purified protein agreed with the predicted values based on the DNA sequence of the gene. Furthermore the native molecular weight measured by gel filtration confirmed that asparagine synthetase exists as a dimer of identical subunits.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0916-8451
pubmed:author
pubmed:issnType
Print
pubmed:volume
56
pubmed:geneSymbol
asnA
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
376-9
pubmed:dateRevised
2006-5-1
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Overexpression and purification of asparagine synthetase from Escherichia coli.
pubmed:affiliation
Institute for Chemical Research, Kyoto University.
pubmed:publicationType
Journal Article