Linked Life Data

6874870

Source:http://linkedlifedata.com/resource/pubmed/id/6874870

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1983-9-23
pubmed:abstractText
The hydrophobic protein elastin, which is a major constituent of vascular and lung tissue is fragmented in several pathological conditions. The nature of the soluble fragments is not well understood. Such fragments bind to alkyl chains linked to agarose. Elution, which is effected by dimethylformamide and sodium dodecyl sulphate, is optimal from the decyl-agarose column. Dialysis of the eluates against buffered sodium chloride precipitates elastin, thus further purifying the salt-soluble cross-linked elastin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31-40
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Purification of salt-soluble cross-linked elastin by hydrophobic interaction chromatography.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't