Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-6-4
pubmed:abstractText
A highly efficient expression for human acidic fibroblast growth factor (aFGF) has been assembled to direct the synthesis of both shortened and native full-length aFGF. The full-length aFGF-154 form of the protein had not been produced before in Escherichia coli by genetic engineering, and is obtained with its initiator methionine removed. The high production of the aFGF allows one to circumvent the use of reversed-phase chromatography (RPC) during the purification procedure. Here, it is shown that RPC, routinely used to obtain pure preparations of recombinant aFGF, modifies its chemical and physical properties in an unfavorable manner.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
113
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
231-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:1374047-3T3 Cells, pubmed-meshheading:1374047-Amino Acids, pubmed-meshheading:1374047-Animals, pubmed-meshheading:1374047-Base Sequence, pubmed-meshheading:1374047-Chromatography, High Pressure Liquid, pubmed-meshheading:1374047-Circular Dichroism, pubmed-meshheading:1374047-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:1374047-Escherichia coli, pubmed-meshheading:1374047-Fibroblast Growth Factor 1, pubmed-meshheading:1374047-Genes, Bacterial, pubmed-meshheading:1374047-Genetic Vectors, pubmed-meshheading:1374047-Humans, pubmed-meshheading:1374047-Mice, pubmed-meshheading:1374047-Mice, Inbred BALB C, pubmed-meshheading:1374047-Molecular Sequence Data, pubmed-meshheading:1374047-Plasmids, pubmed-meshheading:1374047-Recombinant Proteins, pubmed-meshheading:1374047-Solutions, pubmed-meshheading:1374047-Spectrometry, Fluorescence
pubmed:year
1992
pubmed:articleTitle
High-level synthesis in Escherichia coli of shortened and full-length human acidic fibroblast growth factor and purification in a form stable in aqueous solutions.
pubmed:affiliation
Centro de Investigaciones Biológicas, C.S.I.C., Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't