Linked Life Data

2730655

Source:http://linkedlifedata.com/resource/pubmed/id/2730655

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-7-12
pubmed:abstractText
Two heparin binding growth factors with different molecular weight, 16.6 kD and 18.6 kD polypeptide, were purified from bovine omentum. The two factors have almost the same affinity to heparin; they were eluted with 1.0 M NaCl from the affinity column. The 16.6 kD polypeptide was found to be acidic fibroblast growth factor by amino acid sequence analysis. The 18.6 kD polypeptide was an N-terminus blocked polypeptide and was suggested to be beta-endothelial cell growth factor. These molecular species may play significant roles in maintaining vascularized structure in omentum and be related to the angiogenic activity of the tissue.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
161
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
169-75
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Purification of acidic fibroblast growth factor from bovine omentum.
pubmed:affiliation
Tsukuba Research Laboratories, Takeda Chemical Industries, Ltd., Ibaraki, Japan.
pubmed:publicationType
Journal Article