| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-78 |
Sentence |
denotes |
Characterization of complex formation between lipopolysaccharide and lysozyme. |
| TextSentencer_T2 |
79-229 |
Sentence |
denotes |
The binding of lysozyme (LZM) to bacterial lipopolysaccharide (LPS) inhibited the biological activities of LPS as well as the enzymic activity of LZM. |
| TextSentencer_T3 |
230-319 |
Sentence |
denotes |
The mode of binding has been characterized by using dansylated LZM and enzyme inhibition. |
| TextSentencer_T4 |
320-599 |
Sentence |
denotes |
The binding of LPS to LZM significantly increased the fluorescence intensity (Fl-intensity) of the danyl group and was found to be time-dependent; the complex was produced gradually and became stabilized within 20 min at 37 degrees, 10 min at 50 degrees, and 1 min at 70 degrees. |
| TextSentencer_T5 |
600-728 |
Sentence |
denotes |
The maximum level of binding was also dependent on the reaction temperature, and more complex was formed at higher temperatures. |
| TextSentencer_T6 |
729-838 |
Sentence |
denotes |
Complexation was strongly dependent on the salt concentration and was not observed at greater than 0.5M NaCl. |
| TextSentencer_T7 |
839-1190 |
Sentence |
denotes |
From collected evidence of the Fl-intensities of various dansyl derivatives and amphiphiles, it is concluded that LZM interacts with LPS by multiple binding-modes, the first being strongly related to the enzyme inhibition, the second being close to the Fl-intensity, and the third being dependent on the inhibition of immunopharmacological activities. |
| TextSentencer_T8 |
1191-1482 |
Sentence |
denotes |
For the amphiphiles used in this study, sodium dodecyl sulfate (SDS), 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), 3-[(3-cholamidopropyl)dimethylammonio]-2-hydroxy-propanesulfonate (CHAPSO), decansulfonic acid, and cardiolipin have binding modes similar to that of LPS. |
| T1 |
0-78 |
Sentence |
denotes |
Characterization of complex formation between lipopolysaccharide and lysozyme. |
| T2 |
79-229 |
Sentence |
denotes |
The binding of lysozyme (LZM) to bacterial lipopolysaccharide (LPS) inhibited the biological activities of LPS as well as the enzymic activity of LZM. |
| T3 |
230-319 |
Sentence |
denotes |
The mode of binding has been characterized by using dansylated LZM and enzyme inhibition. |
| T4 |
320-599 |
Sentence |
denotes |
The binding of LPS to LZM significantly increased the fluorescence intensity (Fl-intensity) of the danyl group and was found to be time-dependent; the complex was produced gradually and became stabilized within 20 min at 37 degrees, 10 min at 50 degrees, and 1 min at 70 degrees. |
| T5 |
600-728 |
Sentence |
denotes |
The maximum level of binding was also dependent on the reaction temperature, and more complex was formed at higher temperatures. |
| T6 |
729-838 |
Sentence |
denotes |
Complexation was strongly dependent on the salt concentration and was not observed at greater than 0.5M NaCl. |
| T7 |
839-1190 |
Sentence |
denotes |
From collected evidence of the Fl-intensities of various dansyl derivatives and amphiphiles, it is concluded that LZM interacts with LPS by multiple binding-modes, the first being strongly related to the enzyme inhibition, the second being close to the Fl-intensity, and the third being dependent on the inhibition of immunopharmacological activities. |
| T8 |
1191-1482 |
Sentence |
denotes |
For the amphiphiles used in this study, sodium dodecyl sulfate (SDS), 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), 3-[(3-cholamidopropyl)dimethylammonio]-2-hydroxy-propanesulfonate (CHAPSO), decansulfonic acid, and cardiolipin have binding modes similar to that of LPS. |