Pub. Date : 1995 Jan 15
PMID : 7851434
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The highly purified (greater than 95%) stable fusion protein, obtained by affinity chromatography, was very active in enhancing the dissociation rate or the GDP/GTP exchange of the GDP complex of Ras2p or human H-ras p21. | Guanosine Diphosphate | Ras family GTPase RAS2 | Saccharomyces cerevisiae S288C |
| 2 | The highly purified (greater than 95%) stable fusion protein, obtained by affinity chromatography, was very active in enhancing the dissociation rate or the GDP/GTP exchange of the GDP complex of Ras2p or human H-ras p21. | Guanosine Diphosphate | Ras family GTPase RAS2 | Saccharomyces cerevisiae S288C |
| 3 | The stimulation of the guanine nucleotide release by Sdc25p-C was stronger for Ras2p.GDP than Ras2p.GTP, an effect that was less pronounced in the case of the p21 complexes. | Guanosine Diphosphate | Ras family GTPase RAS2 | Saccharomyces cerevisiae S288C |
| 4 | The association rate of the Ras2p.GDP (GTP) complex was also enhanced by Sdc25p-C. Monovalent and divalent salts inhibit the nucleotide-releasing activity of Sdc25p-C. | Guanosine Diphosphate | Ras family GTPase RAS2 | Saccharomyces cerevisiae S288C |
| 5 | On gel filtration, truncated Sdc25p-C and nucleotide-free Ras2p (or p21) formed a stable 1:1 stoichiometric complex that was dissociated by increasing concentrations of GDP. | Guanosine Diphosphate | Ras family GTPase RAS2 | Saccharomyces cerevisiae S288C |
| 6 | The complex with [S24N]Ras2p was greater than 100-fold less sensitive to the dissociating effect of GDP, whereas [R80D, N81D]Ras2p was unable to form a stable complex with truncated Sdc25p-C. | Guanosine Diphosphate | Ras family GTPase RAS2 | Saccharomyces cerevisiae S288C |