Linked Life Data

12656349

Source:http://linkedlifedata.com/resource/pubmed/id/12656349

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-3-26
pubmed:abstractText
Human acidic and basic fibroblast growth factors (aFGF and bFGF) are classic and well characterized members of the heparin-binding growth factor family. Heparin is generally thought to play an extremely important role in regulating aFGF and bFGF bioactivities through its strong binding with them. In order to unravel the mechanism of the interactions between heparin and FGFs, and evaluate the importance of heparin sulfate groups' binding with FGFs, surface plasmon resonance analyses were performed using IAsys Cuvettes System. Heparin and its regioselectively desulfated derivatives were immobilized on the cuvettes. aFGF and bFGF solutions with different concentrations were pipetted into the cuvettes and the progress of the interaction was monitored in real-time by Windows-based software, yielding kinetic and equilibrium constants for these interactions. In addition, in order to reduce the delicate difference among the cuvettes, inhibition analyses of mixture of FGFs and immobilized native heparin by modified heparins were also done. The data from these two methods were similar, indicating that all sulfate groups at 2-O, 6-O and N- in heparin were required for the binding to aFGF; and that their contribution to the binding was in the order 2-O, N- and 6-O-sulfate group. In contrast, definite contribution of the 6-O-sulfate group to the binding with bFGF was most apparent, while the other two sulfate groups appeared to be necessary in the order 2-O and N-sulfate group. These methods established here can be used for analysing the effect of sulfate groups in heparin on the binding with other human FGF members or other heparin-binding proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1009-3095
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
86-94
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Surface plasmon resonance analysis to evaluate the importance of heparin sulfate groups' binding with human aFGF and bFGF.
pubmed:affiliation
College of Animal Sciences, Zhejiang University, Huajiachi Campus, Hangzhou 310029, China. wuxiaofeng@zju.edu.cn
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't