FLUOROSPECTROMETRIC ANALYSIS OF HEPARIN INTERACTION WITH FIBROBLAST GROWTH-FACTORS

被引：11

作者：

LI, LY

SEDDON, AP

机构：

[1] Department of Protein Chemistry Medical Research Division, American Cyanamid Company, Pearl River

来源：

GROWTH FACTORS | 1994年 / 11卷 / 01期

关键词：

HEPARIN; HEPARAN SULFATE PROTEOGLYCANS; FIBROBLAST GROWTH FACTORS; FLUORESCENCE QUENCHING; FLUOROSPECTROSCOPY;

D O I：

10.3109/08977199409015046

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The fluorescence emission of a single tryptophan residue present in both FGF-1 and FGF-2 was used as a structural probe to directly assess the interaction of the growth factors with heparin or beta-cyclodextran tetradecasulfate. About 20-25% of the fluorescence of either FGF-1 or FGF-2 is quenchable, and is dependent on sulfation of the ligands. The quenchable fluorescence is associated with about 20% of total FGF, suggesting the presence of two fluorospectrometric forms of the protein. The equilibrium dissociation constants, deter mined by this method, for heparin or beta-cyclodextrin tetradecasulfate binding to FGF-1 are about 1 nM, whereas the values for FGF-2 are 1 and 23 nM, respectively. The method provides a direct tool to evaluate FGF-ligand interaction and assess the structural integrity of the proteins.

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页码：1 / 7

页数：7

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