| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-134 |
Sentence |
denotes |
Ca2+ binding to the first epidermal growth factor-like domain of factor VIIa increases amidolytic activity and tissue factor affinity. |
| T2 |
135-430 |
Sentence |
denotes |
Coagulation factor VIIa belongs to a family of homologous enzymes, including factors IXa and Xa and activated protein C, composed of two epidermal growth factor-like domains located between an N-terminal domain rich in gamma-carboxyglutamic acid residues and a C-terminal serine protease domain. |
| T3 |
431-563 |
Sentence |
denotes |
The first epidermal growth factor-like domain in factor VIIa contains a Ca2+ binding site, the function of which is largely unknown. |
| T4 |
564-753 |
Sentence |
denotes |
Site-directed mutagenesis of two Ca2+-liganding Asp residues in this domain abolished Ca2+ binding and resulted in a 2-3-fold decrease in amidolytic activity at optimal Ca2+ concentrations. |
| T5 |
754-890 |
Sentence |
denotes |
The lower amidolytic activity persisted in complex with soluble tissue factor, apparently due to a lower kcat of the mutant factor VIIa. |
| T6 |
891-1003 |
Sentence |
denotes |
Mutant and wild-type factor VIIa bound to lipidated tissue factor were equally efficient activators of factor X. |
| T7 |
1004-1237 |
Sentence |
denotes |
The dissociation constants, derived from amidolytic activity and surface plasmon resonance measurements, were 2-5 nM and 50-60 nM for the interactions between wild-type and mutant factor VIIa, respectively, and soluble tissue factor. |
| T8 |
1238-1381 |
Sentence |
denotes |
Binding to lipidated tissue factor was characterized by dissociation constants of 7.5 pM for factor VIIa and 160 pM for the factor VIIa mutant. |
| T9 |
1382-1579 |
Sentence |
denotes |
Hence, a functional Ca2+ binding site in the first epidermal growth factor-like domain added 7-8 kJ/mol to the total binding energy of the interaction with both lipidated and soluble tissue factor. |
| T1 |
0-134 |
Sentence |
denotes |
Ca2+ binding to the first epidermal growth factor-like domain of factor VIIa increases amidolytic activity and tissue factor affinity. |
| T2 |
135-430 |
Sentence |
denotes |
Coagulation factor VIIa belongs to a family of homologous enzymes, including factors IXa and Xa and activated protein C, composed of two epidermal growth factor-like domains located between an N-terminal domain rich in gamma-carboxyglutamic acid residues and a C-terminal serine protease domain. |
| T3 |
431-563 |
Sentence |
denotes |
The first epidermal growth factor-like domain in factor VIIa contains a Ca2+ binding site, the function of which is largely unknown. |
| T4 |
564-753 |
Sentence |
denotes |
Site-directed mutagenesis of two Ca2+-liganding Asp residues in this domain abolished Ca2+ binding and resulted in a 2-3-fold decrease in amidolytic activity at optimal Ca2+ concentrations. |
| T5 |
754-890 |
Sentence |
denotes |
The lower amidolytic activity persisted in complex with soluble tissue factor, apparently due to a lower kcat of the mutant factor VIIa. |
| T6 |
891-1003 |
Sentence |
denotes |
Mutant and wild-type factor VIIa bound to lipidated tissue factor were equally efficient activators of factor X. |
| T7 |
1004-1237 |
Sentence |
denotes |
The dissociation constants, derived from amidolytic activity and surface plasmon resonance measurements, were 2-5 nM and 50-60 nM for the interactions between wild-type and mutant factor VIIa, respectively, and soluble tissue factor. |
| T8 |
1238-1381 |
Sentence |
denotes |
Binding to lipidated tissue factor was characterized by dissociation constants of 7.5 pM for factor VIIa and 160 pM for the factor VIIa mutant. |
| T9 |
1382-1579 |
Sentence |
denotes |
Hence, a functional Ca2+ binding site in the first epidermal growth factor-like domain added 7-8 kJ/mol to the total binding energy of the interaction with both lipidated and soluble tissue factor. |
