| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-169 |
Sentence |
denotes |
Hyaluronan synthase assembles hyaluronan on a [GlcNAc(β1,4)]n-GlcNAc(α1→)UDP primer and hyaluronan retains this residual chitin oligomer as a cap at the nonreducing end. |
| T1 |
0-169 |
Sentence |
denotes |
Hyaluronan synthase assembles hyaluronan on a [GlcNAc(β1,4)]n-GlcNAc(α1→)UDP primer and hyaluronan retains this residual chitin oligomer as a cap at the nonreducing end. |
| TextSentencer_T2 |
170-286 |
Sentence |
denotes |
Class I hyaluronan synthases (HAS) assemble [GlcNAc(β1,4)GlcUA(β1,3)]n-UDP at the reducing end and also make chitin. |
| T2 |
170-286 |
Sentence |
denotes |
Class I hyaluronan synthases (HAS) assemble [GlcNAc(β1,4)GlcUA(β1,3)]n-UDP at the reducing end and also make chitin. |
| TextSentencer_T3 |
287-415 |
Sentence |
denotes |
Streptococcus equisimilis HAS (SeHAS) also synthesizes chitin-UDP oligosaccharides, (GlcNAc-β1,4)n-GlcNAc(α1→)UDP (Weigel et al. |
| T3 |
287-415 |
Sentence |
denotes |
Streptococcus equisimilis HAS (SeHAS) also synthesizes chitin-UDP oligosaccharides, (GlcNAc-β1,4)n-GlcNAc(α1→)UDP (Weigel et al. |
| TextSentencer_T4 |
416-422 |
Sentence |
denotes |
2015). |
| T4 |
416-422 |
Sentence |
denotes |
2015). |
| TextSentencer_T5 |
423-557 |
Sentence |
denotes |
Here we determined if HAS uses chitin-UDPs as primers to initiate HA synthesis, leaving the non-HA primer at the nonreducing (NR) end. |
| T5 |
423-557 |
Sentence |
denotes |
Here we determined if HAS uses chitin-UDPs as primers to initiate HA synthesis, leaving the non-HA primer at the nonreducing (NR) end. |
| TextSentencer_T6 |
558-728 |
Sentence |
denotes |
HA made by SeHAS membranes was purified, digested with streptomyces lyase, and hydrophobic oligomers were enriched by solid phase extraction and analyzed by MALDI-TOF MS. |
| T6 |
558-728 |
Sentence |
denotes |
HA made by SeHAS membranes was purified, digested with streptomyces lyase, and hydrophobic oligomers were enriched by solid phase extraction and analyzed by MALDI-TOF MS. |
| TextSentencer_T7 |
729-937 |
Sentence |
denotes |
Jack bean hexosaminidase (JBH) and MS/MS were used to analyze 19 m/z species of possible GnHn ions with clustered GlcNAc (G) residues attached to disaccharide units (H): (GlcNAcβ1,4)2-5[GlcUA(β1,3)GlcNAc]2-6. |
| T7 |
729-937 |
Sentence |
denotes |
Jack bean hexosaminidase (JBH) and MS/MS were used to analyze 19 m/z species of possible GnHn ions with clustered GlcNAc (G) residues attached to disaccharide units (H): (GlcNAcβ1,4)2-5[GlcUA(β1,3)GlcNAc]2-6. |
| TextSentencer_T8 |
938-1068 |
Sentence |
denotes |
JBH digestion sequentially removed GlcNAc from the NR-end of GnHn oligomers, producing successively smaller GnH2-3 series members. |
| T8 |
938-1068 |
Sentence |
denotes |
JBH digestion sequentially removed GlcNAc from the NR-end of GnHn oligomers, producing successively smaller GnH2-3 series members. |
| TextSentencer_T9 |
1069-1167 |
Sentence |
denotes |
Since lyase releases dehydro-oligos (dHn; M-18), only the unique NR-end oligo lacks dehydro-GlcUA. |
| T9 |
1069-1167 |
Sentence |
denotes |
Since lyase releases dehydro-oligos (dHn; M-18), only the unique NR-end oligo lacks dehydro-GlcUA. |
| TextSentencer_T10 |
1168-1307 |
Sentence |
denotes |
Hn oligomers were undetectable in lyase digests, whereas JBH treatment created new H2-6m/z peaks (i.e. HA tetra- through dodeca-oligomers). |
| T10 |
1168-1307 |
Sentence |
denotes |
Hn oligomers were undetectable in lyase digests, whereas JBH treatment created new H2-6m/z peaks (i.e. HA tetra- through dodeca-oligomers). |
| TextSentencer_T11 |
1308-1436 |
Sentence |
denotes |
MS/MS of larger GnHn species produced chitin (2-5 GlcNAcs), HA oligomers and multiple smaller series members with fewer GlcNAcs. |
| T11 |
1308-1436 |
Sentence |
denotes |
MS/MS of larger GnHn species produced chitin (2-5 GlcNAcs), HA oligomers and multiple smaller series members with fewer GlcNAcs. |
| TextSentencer_T12 |
1437-1603 |
Sentence |
denotes |
All NR-ends (97%) started with GlcNAc, as a chitin trimer (three GlcNAcs), indicating that GlcNAc(β1,4)2GlcNAc(α1→)-UDP may be optimal for initiation of HA synthesis. |
| T12 |
1437-1603 |
Sentence |
denotes |
All NR-ends (97%) started with GlcNAc, as a chitin trimer (three GlcNAcs), indicating that GlcNAc(β1,4)2GlcNAc(α1→)-UDP may be optimal for initiation of HA synthesis. |
| TextSentencer_T13 |
1604-1674 |
Sentence |
denotes |
Also, HA made by live S. pyogenes cells had G4Hn chitin-oligo NR-ends. |
| T13 |
1604-1674 |
Sentence |
denotes |
Also, HA made by live S. pyogenes cells had G4Hn chitin-oligo NR-ends. |
| TextSentencer_T14 |
1675-1887 |
Sentence |
denotes |
We conclude that chitin-UDP functions in vitro and in live cells as a primer to initiate synthesis of all HA chains and these primers remain at the NR-ends of HA chains as residual chitin caps [(GlcNAc-β1,4)3-4]. |
| T14 |
1675-1887 |
Sentence |
denotes |
We conclude that chitin-UDP functions in vitro and in live cells as a primer to initiate synthesis of all HA chains and these primers remain at the NR-ends of HA chains as residual chitin caps [(GlcNAc-β1,4)3-4]. |