| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-102 |
Sentence |
denotes |
Production and characterization of a monomeric form and a single-site form of Aleuria aurantia lectin. |
| T1 |
0-102 |
Sentence |
denotes |
Production and characterization of a monomeric form and a single-site form of Aleuria aurantia lectin. |
| T1 |
0-102 |
Sentence |
denotes |
Production and characterization of a monomeric form and a single-site form of Aleuria aurantia lectin. |
| TextSentencer_T2 |
103-195 |
Sentence |
denotes |
Lectins have widely been used in structural and functional studies of complex carbohydrates. |
| T2 |
103-195 |
Sentence |
denotes |
Lectins have widely been used in structural and functional studies of complex carbohydrates. |
| T2 |
103-195 |
Sentence |
denotes |
Lectins have widely been used in structural and functional studies of complex carbohydrates. |
| TextSentencer_T3 |
196-298 |
Sentence |
denotes |
They usually bind carbohydrates with relatively low affinity, but compensate for this by multivalency. |
| T3 |
196-298 |
Sentence |
denotes |
They usually bind carbohydrates with relatively low affinity, but compensate for this by multivalency. |
| T3 |
196-298 |
Sentence |
denotes |
They usually bind carbohydrates with relatively low affinity, but compensate for this by multivalency. |
| TextSentencer_T4 |
299-501 |
Sentence |
denotes |
This multivalent nature of lectins can sometimes produce unwanted reactions such as agglutination or precipitation of target glycoproteins, when using them in different biological and analytical assays. |
| T4 |
299-501 |
Sentence |
denotes |
This multivalent nature of lectins can sometimes produce unwanted reactions such as agglutination or precipitation of target glycoproteins, when using them in different biological and analytical assays. |
| T4 |
299-501 |
Sentence |
denotes |
This multivalent nature of lectins can sometimes produce unwanted reactions such as agglutination or precipitation of target glycoproteins, when using them in different biological and analytical assays. |
| TextSentencer_T5 |
502-583 |
Sentence |
denotes |
The mushroom lectin Aleuria aurantia binds to fucose-containing oligosaccharides. |
| T5 |
502-583 |
Sentence |
denotes |
The mushroom lectin Aleuria aurantia binds to fucose-containing oligosaccharides. |
| T5 |
502-583 |
Sentence |
denotes |
The mushroom lectin Aleuria aurantia binds to fucose-containing oligosaccharides. |
| TextSentencer_T6 |
584-682 |
Sentence |
denotes |
It is composed of two identical subunits, and each subunit contains five binding sites for fucose. |
| T6 |
584-682 |
Sentence |
denotes |
It is composed of two identical subunits, and each subunit contains five binding sites for fucose. |
| T6 |
584-682 |
Sentence |
denotes |
It is composed of two identical subunits, and each subunit contains five binding sites for fucose. |
| TextSentencer_T7 |
683-773 |
Sentence |
denotes |
In this study, two forms of recombinant AAL were produced using site-directed mutagenesis. |
| T7 |
683-773 |
Sentence |
denotes |
In this study, two forms of recombinant AAL were produced using site-directed mutagenesis. |
| T7 |
683-773 |
Sentence |
denotes |
In this study, two forms of recombinant AAL were produced using site-directed mutagenesis. |
| TextSentencer_T8 |
774-985 |
Sentence |
denotes |
A monomeric form of AAL was produced by exchanging Tyr6 with Arg6, and a single-site fragment of AAL was produced by insertion of an NdeI restriction enzyme cleavage site and a stop codon in the coding sequence. |
| T8 |
774-985 |
Sentence |
denotes |
A monomeric form of AAL was produced by exchanging Tyr6 with Arg6, and a single-site fragment of AAL was produced by insertion of an NdeI restriction enzyme cleavage site and a stop codon in the coding sequence. |
| T8 |
774-985 |
Sentence |
denotes |
A monomeric form of AAL was produced by exchanging Tyr6 with Arg6, and a single-site fragment of AAL was produced by insertion of an NdeI restriction enzyme cleavage site and a stop codon in the coding sequence. |
| TextSentencer_T9 |
986-1098 |
Sentence |
denotes |
The AAL forms were expressed as His-tagged proteins in Escherichia coli and purified by affinity chromatography. |
| T9 |
986-1098 |
Sentence |
denotes |
The AAL forms were expressed as His-tagged proteins in Escherichia coli and purified by affinity chromatography. |
| T9 |
986-1098 |
Sentence |
denotes |
The AAL forms were expressed as His-tagged proteins in Escherichia coli and purified by affinity chromatography. |
| TextSentencer_T10 |
1099-1260 |
Sentence |
denotes |
Binding properties of the two AAL forms were performed using surface plasmon resonance, enzyme-linked lectin assay analyses and isothermal titration calorimetry. |
| T10 |
1099-1260 |
Sentence |
denotes |
Binding properties of the two AAL forms were performed using surface plasmon resonance, enzyme-linked lectin assay analyses and isothermal titration calorimetry. |
| T10 |
1099-1260 |
Sentence |
denotes |
Binding properties of the two AAL forms were performed using surface plasmon resonance, enzyme-linked lectin assay analyses and isothermal titration calorimetry. |
| TextSentencer_T11 |
1261-1391 |
Sentence |
denotes |
Both the monomeric AAL (mAAL) and the single-site AAL (S2-AAL) forms retained their capacity to bind fucosylated oligosaccharides. |
| T11 |
1261-1391 |
Sentence |
denotes |
Both the monomeric AAL (mAAL) and the single-site AAL (S2-AAL) forms retained their capacity to bind fucosylated oligosaccharides. |
| T11 |
1261-1391 |
Sentence |
denotes |
Both the monomeric AAL (mAAL) and the single-site AAL (S2-AAL) forms retained their capacity to bind fucosylated oligosaccharides. |
| TextSentencer_T12 |
1392-1611 |
Sentence |
denotes |
However, both constructs exhibited properties that differed from the intact recombinant AAL (rAAL). mAAL showed similar binding affinities to fucosylated oligosaccharides as rAAL, but had less hemagglutinating capacity. |
| T12 |
1392-1611 |
Sentence |
denotes |
However, both constructs exhibited properties that differed from the intact recombinant AAL (rAAL). mAAL showed similar binding affinities to fucosylated oligosaccharides as rAAL, but had less hemagglutinating capacity. |
| T12 |
1392-1611 |
Sentence |
denotes |
However, both constructs exhibited properties that differed from the intact recombinant AAL (rAAL). mAAL showed similar binding affinities to fucosylated oligosaccharides as rAAL, but had less hemagglutinating capacity. |
| TextSentencer_T13 |
1612-1774 |
Sentence |
denotes |
S2-AAL showed a lower binding affinity to fucosylated oligosaccharides and, in contrast to rAAL and mAAL, S2-AAL did not bind to sialylated fuco-oligosaccharides. |
| T13 |
1612-1774 |
Sentence |
denotes |
S2-AAL showed a lower binding affinity to fucosylated oligosaccharides and, in contrast to rAAL and mAAL, S2-AAL did not bind to sialylated fuco-oligosaccharides. |
| T13 |
1612-1774 |
Sentence |
denotes |
S2-AAL showed a lower binding affinity to fucosylated oligosaccharides and, in contrast to rAAL and mAAL, S2-AAL did not bind to sialylated fuco-oligosaccharides. |
| TextSentencer_T14 |
1775-1960 |
Sentence |
denotes |
The study shows that molecular engineering is a highly useful tool for producing lectins with more defined properties such as decreased valency and defined specificities and affinities. |
| T14 |
1775-1960 |
Sentence |
denotes |
The study shows that molecular engineering is a highly useful tool for producing lectins with more defined properties such as decreased valency and defined specificities and affinities. |
| T14 |
1775-1960 |
Sentence |
denotes |
The study shows that molecular engineering is a highly useful tool for producing lectins with more defined properties such as decreased valency and defined specificities and affinities. |
| TextSentencer_T15 |
1961-2082 |
Sentence |
denotes |
Thus, this approach has high potential in developing reliable diagnostic and biological assays for carbohydrate analysis. |
| T15 |
1961-2082 |
Sentence |
denotes |
Thus, this approach has high potential in developing reliable diagnostic and biological assays for carbohydrate analysis. |
| T15 |
1961-2082 |
Sentence |
denotes |
Thus, this approach has high potential in developing reliable diagnostic and biological assays for carbohydrate analysis. |