| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-47 |
Sentence |
denotes |
N-glycosylation of ovomucin from hen egg white. |
| T1 |
0-47 |
Sentence |
denotes |
N-glycosylation of ovomucin from hen egg white. |
| TextSentencer_T2 |
48-248 |
Sentence |
denotes |
Ovomucin is a bioactive egg white glycoprotein responsible for the gel properties of fresh egg white and is believed to be involved in egg white thinning, a natural process that occurs during storage. |
| T2 |
48-248 |
Sentence |
denotes |
Ovomucin is a bioactive egg white glycoprotein responsible for the gel properties of fresh egg white and is believed to be involved in egg white thinning, a natural process that occurs during storage. |
| TextSentencer_T3 |
249-421 |
Sentence |
denotes |
Ovomucin is composed of two subunits: a carbohydrate-rich β-ovomucin with molecular weight of 400-610 KDa and a carbohydrate-poor α-ovomucin with molecular mass of 254 KDa. |
| T3 |
249-421 |
Sentence |
denotes |
Ovomucin is composed of two subunits: a carbohydrate-rich β-ovomucin with molecular weight of 400-610 KDa and a carbohydrate-poor α-ovomucin with molecular mass of 254 KDa. |
| TextSentencer_T4 |
422-571 |
Sentence |
denotes |
In addition to limited information on O-linked glycans of ovomucin, there is no study on either the N-glycan structures or the N-glycosylation sites. |
| T4 |
422-571 |
Sentence |
denotes |
In addition to limited information on O-linked glycans of ovomucin, there is no study on either the N-glycan structures or the N-glycosylation sites. |
| TextSentencer_T5 |
572-714 |
Sentence |
denotes |
The purpose of the present study was to characterize the N-glycosylation of ovomucin from fresh eggs using nano LC ESI-MS, MS/MS and MALDI MS. |
| T5 |
572-714 |
Sentence |
denotes |
The purpose of the present study was to characterize the N-glycosylation of ovomucin from fresh eggs using nano LC ESI-MS, MS/MS and MALDI MS. |
| TextSentencer_T6 |
715-789 |
Sentence |
denotes |
Our results showed the presence of N-linked glycans on both glycoproteins. |
| T6 |
715-789 |
Sentence |
denotes |
Our results showed the presence of N-linked glycans on both glycoproteins. |
| TextSentencer_T7 |
790-848 |
Sentence |
denotes |
We found 18 potential N-glycosylation sites in α-ovomucin. |
| T7 |
790-848 |
Sentence |
denotes |
We found 18 potential N-glycosylation sites in α-ovomucin. |
| TextSentencer_T8 |
849-1004 |
Sentence |
denotes |
15 sites were glycosylated, one site was found in both glycosylated and non-glycosylated forms and two potential glycosylation sites were found unoccupied. |
| T8 |
849-1004 |
Sentence |
denotes |
15 sites were glycosylated, one site was found in both glycosylated and non-glycosylated forms and two potential glycosylation sites were found unoccupied. |
| TextSentencer_T9 |
1005-1129 |
Sentence |
denotes |
The N-glycans of α-ovomucin found on the glycosylation sites are complex-type structures with bisecting N-acetylglucosamine. |
| T9 |
1005-1129 |
Sentence |
denotes |
The N-glycans of α-ovomucin found on the glycosylation sites are complex-type structures with bisecting N-acetylglucosamine. |
| TextSentencer_T10 |
1130-1292 |
Sentence |
denotes |
MALDI MS of the N-glycans released from α-ovomucin by PNGase F revealed that the most abundant glycan structure is a bisected type of composition GlcNAc(6)Man(3). |
| T10 |
1130-1292 |
Sentence |
denotes |
MALDI MS of the N-glycans released from α-ovomucin by PNGase F revealed that the most abundant glycan structure is a bisected type of composition GlcNAc(6)Man(3). |
| TextSentencer_T11 |
1293-1343 |
Sentence |
denotes |
Two N-glycosylated sites were found in β-ovomucin. |
| T11 |
1293-1343 |
Sentence |
denotes |
Two N-glycosylated sites were found in β-ovomucin. |
