Linked Life Data

1783658

Source:http://linkedlifedata.com/resource/pubmed/id/1783658

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-3-19
pubmed:abstractText
A recombinant mycobacterial heat shock protein of relative molecular mass 60,000 was purified by hydrophobic interaction chromatography. Chromatographic media with ligands of medium hydrophobicity, such as phenyl-Sepharose, bound too strongly to be used for the purification of this heat shock protein. Butyl-Sepharose, with weak hydrophobicity, allowed binding and elution with decreasing concentrations of ammonium sulphate, but only alkyl-Superose allowed the separation of two similar proteins from the Escherichia coli clone expressing the recombinant heat shock protein (relative molecular mass 60,000) of Mycobacterium bovis BCG. The binding parameters of recombinant human heat shock proteins of relative molecular mass 60,000 and 70,000 indicate that phenyl-Sepharose also binds too strongly for the separation of these two heat shock proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
587
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19-23
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Hydrophobic interaction chromatography for the purification of a mycobacterial heat shock protein of relative molecular mass 60,000.
pubmed:affiliation
Department of Immunology, University of Ulm, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't