Pub. Date : 1993 May 15
PMID : 8508806
14 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Biochemical bases of the interaction of human basic fibroblast growth factor with glycosaminoglycans. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |
| 2 | In the present study we have attempted a characterization of the biochemical bases of the interaction of human basic fibroblast growth factor (bFGF) with glycosaminoglycans (GAGs) in solution. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |
| 3 | In the present study we have attempted a characterization of the biochemical bases of the interaction of human basic fibroblast growth factor (bFGF) with glycosaminoglycans (GAGs) in solution. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |
| 4 | In the present study we have attempted a characterization of the biochemical bases of the interaction of human basic fibroblast growth factor (bFGF) with glycosaminoglycans (GAGs) in solution. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |
| 5 | In the present study we have attempted a characterization of the biochemical bases of the interaction of human basic fibroblast growth factor (bFGF) with glycosaminoglycans (GAGs) in solution. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |
| 6 | This interaction has been evidenced as the capacity of different GAGs and various sulfated compounds to protect bFGF and different bFGF mutants from tryptic cleavage. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |
| 7 | This interaction has been evidenced as the capacity of different GAGs and various sulfated compounds to protect bFGF and different bFGF mutants from tryptic cleavage. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |
| 8 | The capacity of different GAGs to protect bFGF from proteolytic cleavage decreases in the following order: heparin > heparan sulfate > dermatan sulfate = chondroitin sulfates A and C > hyaluronic acid = K5 polysaccharide, indicating that both the degree of sulfation and the backbone structure of GAG modulate its interaction with bFGF. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |
| 9 | The capacity of different GAGs to protect bFGF from proteolytic cleavage decreases in the following order: heparin > heparan sulfate > dermatan sulfate = chondroitin sulfates A and C > hyaluronic acid = K5 polysaccharide, indicating that both the degree of sulfation and the backbone structure of GAG modulate its interaction with bFGF. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |
| 10 | The capacity of different GAGs to protect bFGF from proteolytic cleavage decreases in the following order: heparin > heparan sulfate > dermatan sulfate = chondroitin sulfates A and C > hyaluronic acid = K5 polysaccharide, indicating that both the degree of sulfation and the backbone structure of GAG modulate its interaction with bFGF. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |
| 11 | The capacity of different GAGs to protect bFGF from proteolytic cleavage decreases in the following order: heparin > heparan sulfate > dermatan sulfate = chondroitin sulfates A and C > hyaluronic acid = K5 polysaccharide, indicating that both the degree of sulfation and the backbone structure of GAG modulate its interaction with bFGF. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |
| 12 | Moreover, tryptic digestion studies performed with various heparin molecules and dextran sulfates of different size, ranging from 2.0 kDa to 500 kDa, indicate that the number of bFGF molecules which interact with a single molecule of polysaccharide is related to the molecular mass of the GAG and that six hexose residues are sufficient to protect 1-2 molecules bFGF. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |
| 13 | In conclusion, our findings indicate that the capacity of GAGs to protect bFGF from tryptic cleavage depends upon their size, sulfation, distribution of the anionic sites along the chain, and structural requirements of the bFGF molecule. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |
| 14 | In conclusion, our findings indicate that the capacity of GAGs to protect bFGF from tryptic cleavage depends upon their size, sulfation, distribution of the anionic sites along the chain, and structural requirements of the bFGF molecule. | Glycosaminoglycans | fibroblast growth factor 2 | Homo sapiens |