Linked Life Data

4043385

Source:http://linkedlifedata.com/resource/pubmed/id/4043385

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-10-31
pubmed:abstractText
Fibronectin from human plasma and its 180 kDa fragment which retained collagen-binding, cell-attachment and heparin-binding activities, were studied by velocity centrifugation and 1H-NMR methods. The fibronectin hydrodynamic radius strongly increased at pH 11 while the hydrodynamic properties of the fragment did not change noticeably. 1H-NMR spectroscopy also showed differences in the molecular properties of fibronectin and its 180 kDa fragment. Under physiological conditions the structure of fibronectin differs from that of its 180 kDa fragment. At pH 11 and in 4 M urea no differences in their structures are observed. It is suggested that interdomain and intersubunit interactions play an important role in maintaining the native conformation of intact fibronectin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
189
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
276-80
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
A comparative study of structural properties of fibronectin and its 180 kDa fragment.
pubmed:publicationType
Journal Article, Comparative Study