Pub. Date : 2003 Aug 1
PMID : 12859981
15 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Mechanism of activation of heparin cofactor II by calcium spirulan. | spirulan | serpin family D member 1 | Homo sapiens |
| 2 | Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII. | spirulan | serpin family D member 1 | Homo sapiens |
| 3 | Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII. | spirulan | serpin family D member 1 | Homo sapiens |
| 4 | Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII. | spirulan | serpin family D member 1 | Homo sapiens |
| 5 | Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII. | spirulan | serpin family D member 1 | Homo sapiens |
| 6 | Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII. | spirulan | serpin family D member 1 | Homo sapiens |
| 7 | Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII. | spirulan | serpin family D member 1 | Homo sapiens |
| 8 | Activation of HCII by Ca-SP was molecular-weight dependent. | spirulan | serpin family D member 1 | Homo sapiens |
| 9 | Furthermore, HD22, an aptamer that binds exosite II of thrombin, produced a concentration-dependent, 15-fold reduction at 5 microM in the rate of thrombin inhibition by HCII with Ca-SP, suggesting that Ca-SP interacts with exosite II of thrombin. | spirulan | serpin family D member 1 | Homo sapiens |
| 10 | Furthermore, HD22, an aptamer that binds exosite II of thrombin, produced a concentration-dependent, 15-fold reduction at 5 microM in the rate of thrombin inhibition by HCII with Ca-SP, suggesting that Ca-SP interacts with exosite II of thrombin. | spirulan | serpin family D member 1 | Homo sapiens |
| 11 | Mutations of Lys173 to Leu (K173L) and Arg189 to Leu (R189L) in the HCII molecule resulted in large decreases in the rate of thrombin inhibition mediated by Ca-SP and in the NaCl concentration needed for elution from Ca-SP-Toyopearl. | spirulan | serpin family D member 1 | Homo sapiens |
| 12 | Mutations of Lys173 to Leu (K173L) and Arg189 to Leu (R189L) in the HCII molecule resulted in large decreases in the rate of thrombin inhibition mediated by Ca-SP and in the NaCl concentration needed for elution from Ca-SP-Toyopearl. | spirulan | serpin family D member 1 | Homo sapiens |
| 13 | These results indicate that Ca-SP binds to the positive charges of Lys173 and Arg189 on the HCII molecule. | spirulan | serpin family D member 1 | Homo sapiens |
| 14 | In the thrombin inhibitory process by HCII, Ca-SP appears to play as a template by binding to both thrombin and HCII. | spirulan | serpin family D member 1 | Homo sapiens |
| 15 | In the thrombin inhibitory process by HCII, Ca-SP appears to play as a template by binding to both thrombin and HCII. | spirulan | serpin family D member 1 | Homo sapiens |