Pub. Date : 1991 Dec 5
PMID : 1761059
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Disulfide-bonded dimerization of fibronectin in vitro. | Disulfides | fibronectin 1 | Homo sapiens |
| 2 | Low concentrations (less than 1 mM) of Fe3+ enhanced the redimerization of fibronectin, suggesting that metal ions may mediate oxidative reactions in the formation of the disulfides. | Disulfides | fibronectin 1 | Homo sapiens |
| 3 | Dimerization of fibronectin took place most effectively at pH greater than or equal to 8.8 but decreased strongly at lower pH, representing more unfavourable conditions for the action of the thiolate anion in the thiol/disulfide exchange reaction. | Disulfides | fibronectin 1 | Homo sapiens |
| 4 | Redimerized fibronectin, however, lost many of its binding properties to macromolecular ligands, suggesting that the disulfide bonding did not entirely regenerate the proper conformation of the protein. | Disulfides | fibronectin 1 | Homo sapiens |
| 5 | SDS/PAGE analysis of the dialyzed urea-denatured/reduced thrombin and plasmin digests of fibronectin revealed that the NH2-terminal 30-kDa fragment and other fragments that contained intrachain disulfides quantitatively regained their non-reduced electrophoretic mobility. | Disulfides | fibronectin 1 | Homo sapiens |
| 6 | The results show that the dimerization and formation of intrachain disulfides of fibronectin may occur, in part, spontaneously, based on the amino acid sequence information of the protein. | Disulfides | fibronectin 1 | Homo sapiens |