Pub. Date : 1989 Feb 25
PMID : 2492530
24 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. | Lysine | serpin family C member 1 | Homo sapiens |
| 2 | Binding of heparin to human antithrombin III activates selective chemical modification at lysine 236. | Lysine | serpin family C member 1 | Homo sapiens |
| 3 | Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III. | Lysine | serpin family C member 1 | Homo sapiens |
| 4 | Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III. | Lysine | serpin family C member 1 | Homo sapiens |
| 5 | Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III. | Lysine | serpin family C member 1 | Homo sapiens |
| 6 | A new water-soluble color reagent, 4-N,N-dimethylaminoazobenzene-4"-isothiocyano-2"-sulfonic acid (S-DABITC), was used to identify lysine residues of antithrombin III which participate in the binding of heparin. | Lysine | serpin family C member 1 | Homo sapiens |
| 7 | Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. | Lysine | serpin family C member 1 | Homo sapiens |
| 8 | Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. | Lysine | serpin family C member 1 | Homo sapiens |
| 9 | Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. | Lysine | serpin family C member 1 | Homo sapiens |
| 10 | At a heparin/antithrombin molar ratio of 1, the extent of shielding of Lys-125 and Lys-136 and the unmasking of Lys-236 were 25-33%. | Lysine | serpin family C member 1 | Homo sapiens |
| 11 | At a heparin/antithrombin molar ratio of 1, the extent of shielding of Lys-125 and Lys-136 and the unmasking of Lys-236 were 25-33%. | Lysine | serpin family C member 1 | Homo sapiens |
| 12 | At a heparin/antithrombin molar ratio of 1, the extent of shielding of Lys-125 and Lys-136 and the unmasking of Lys-236 were 25-33%. | Lysine | serpin family C member 1 | Homo sapiens |
| 13 | We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. | Lysine | serpin family C member 1 | Homo sapiens |
| 14 | We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. | Lysine | serpin family C member 1 | Homo sapiens |
| 15 | We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. | Lysine | serpin family C member 1 | Homo sapiens |
| 16 | We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. | Lysine | serpin family C member 1 | Homo sapiens |
| 17 | We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. | Lysine | serpin family C member 1 | Homo sapiens |
| 18 | We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. | Lysine | serpin family C member 1 | Homo sapiens |
| 19 | We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. | Lysine | serpin family C member 1 | Homo sapiens |
| 20 | We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. | Lysine | serpin family C member 1 | Homo sapiens |
| 21 | We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. | Lysine | serpin family C member 1 | Homo sapiens |
| 22 | We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. | Lysine | serpin family C member 1 | Homo sapiens |
| 23 | We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. | Lysine | serpin family C member 1 | Homo sapiens |
| 24 | We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. | Lysine | serpin family C member 1 | Homo sapiens |