Linked Life Data

3753680

Source:http://linkedlifedata.com/resource/pubmed/id/3753680

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1986-2-28
pubmed:abstractText
The complete amino acid sequences of the heparin-, cell- and DNA-binding domains of bovine plasma fibronectin have been determined. The fragments were generated from the 170-kDa central plasmic fragment by extensive digestion with chymotrypsin, and they contain 268, 300 and 269 amino acid residues, respectively. No half-cystines or cysteines were found in these sequences. A glucosamine-based oligosaccharide group is attached to Asn-108 in the sequence of the DNA-binding domain. Only one of the three types of internal homology found in fibronectin [Petersen et al. (1983) Proc. Natl Acad. Sci. USA 80, 137-141], namely the type III homology, occurs in these three fragments, and each of them consists of approximately three stretches of this type III homology. Part of the arrangement of peptides was derived by comparison with the partial cDNA sequence for human fibronectin recently reported [Kornblihtt et al. (1984) Nucleic Acids Res. 12, 5853-5868].
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
154
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15-29
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Purification and complete primary structures of the heparin-, cell-, and DNA-binding domains of bovine plasma fibronectin.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't