Pub. Date : 1986 Jul 15
PMID : 3722204
9 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Disulfide-bonded polymerization of plasma fibronectin in the presence of metal ions. | Disulfides | fibronectin 1 | Homo sapiens |
| 2 | Incubation of human plasma fibronectin in the presence of low concentrations of FeCl3 or CuSO4 led to the formation of disulfide-bonded multimers as revealed by analysis in sodium dodecyl sulfate-polyacrylamide gel electrophoresis under nonreducing or reducing conditions. | Disulfides | fibronectin 1 | Homo sapiens |
| 3 | When incubated in the presence of FeCl3, the Mr 30,000 NH2-terminal, Mr 40,000 gelatin-binding, and the Mr 120,000-140,000 COOH-terminal fragments of fibronectin formed disulfide-bonded polymers, whereas only the Mr 140,000 fragment was polymerized in the presence of CuSO4. | Disulfides | fibronectin 1 | Homo sapiens |
| 4 | Disulfide-bonded polymers were also formed in the presence of FeCl3 but not CuSO4 when the free sulfhydryl groups of fibronectin were blocked by N-ethylmaleimide. | Disulfides | fibronectin 1 | Homo sapiens |
| 5 | The results suggest that in the presence of CuSO4, disulfide-bonded polymerization of fibronectin may involve predominantly the free sulfhydryl groups, whereas in the presence of FeCl3, also the intramolecular disulfides may exchange to form disulfides between separate fibronectin molecules. | Disulfides | fibronectin 1 | Homo sapiens |
| 6 | The results suggest that in the presence of CuSO4, disulfide-bonded polymerization of fibronectin may involve predominantly the free sulfhydryl groups, whereas in the presence of FeCl3, also the intramolecular disulfides may exchange to form disulfides between separate fibronectin molecules. | Disulfides | fibronectin 1 | Homo sapiens |
| 7 | The results suggest that in the presence of CuSO4, disulfide-bonded polymerization of fibronectin may involve predominantly the free sulfhydryl groups, whereas in the presence of FeCl3, also the intramolecular disulfides may exchange to form disulfides between separate fibronectin molecules. | Disulfides | fibronectin 1 | Homo sapiens |
| 8 | The results suggest that in the presence of CuSO4, disulfide-bonded polymerization of fibronectin may involve predominantly the free sulfhydryl groups, whereas in the presence of FeCl3, also the intramolecular disulfides may exchange to form disulfides between separate fibronectin molecules. | Disulfides | fibronectin 1 | Homo sapiens |
| 9 | Thus, under different conditions, different parts of fibronectin may be susceptible to disulfide-bonded polymerization. | Disulfides | fibronectin 1 | Homo sapiens |