| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-77 |
Sentence |
denotes |
Purification and characterization of an adhesin from Pasteurella haemolytica. |
| T1 |
0-77 |
Sentence |
denotes |
Purification and characterization of an adhesin from Pasteurella haemolytica. |
| T1 |
0-77 |
Sentence |
denotes |
Purification and characterization of an adhesin from Pasteurella haemolytica. |
| TextSentencer_T2 |
78-214 |
Sentence |
denotes |
We purified an adhesin from Pasteurella. haemolytica by affinity chromatography using glutaraldehyde treated rabbit erythrocytes stroma. |
| T2 |
78-214 |
Sentence |
denotes |
We purified an adhesin from Pasteurella. haemolytica by affinity chromatography using glutaraldehyde treated rabbit erythrocytes stroma. |
| T2 |
78-214 |
Sentence |
denotes |
We purified an adhesin from Pasteurella. haemolytica by affinity chromatography using glutaraldehyde treated rabbit erythrocytes stroma. |
| TextSentencer_T3 |
215-436 |
Sentence |
denotes |
The adhesin is a protein of 68 kDa, as determined by SDS-PAGE, and the most abundant amino acids constituting this protein were Gly, Ser, Glx, and Ala, and low concentrations of Cys, Met, and Tyr residues were also found. |
| T3 |
215-436 |
Sentence |
denotes |
The adhesin is a protein of 68 kDa, as determined by SDS-PAGE, and the most abundant amino acids constituting this protein were Gly, Ser, Glx, and Ala, and low concentrations of Cys, Met, and Tyr residues were also found. |
| T3 |
215-436 |
Sentence |
denotes |
The adhesin is a protein of 68 kDa, as determined by SDS-PAGE, and the most abundant amino acids constituting this protein were Gly, Ser, Glx, and Ala, and low concentrations of Cys, Met, and Tyr residues were also found. |
| TextSentencer_T4 |
437-495 |
Sentence |
denotes |
The N-terminal sequence of the adhesin is ANEVNVYIYKQPYLI. |
| T4 |
437-495 |
Sentence |
denotes |
The N-terminal sequence of the adhesin is ANEVNVYIYKQPYLI. |
| T4 |
437-495 |
Sentence |
denotes |
The N-terminal sequence of the adhesin is ANEVNVYIYKQPYLI. |
| TextSentencer_T5 |
496-535 |
Sentence |
denotes |
No carbohydrate residues were detected. |
| T5 |
496-535 |
Sentence |
denotes |
No carbohydrate residues were detected. |
| T5 |
496-535 |
Sentence |
denotes |
No carbohydrate residues were detected. |
| TextSentencer_T6 |
536-679 |
Sentence |
denotes |
The adhesin agglutinated rabbit erythrocytes but when the latter were desialylated or pronase treated the agglutinating activity was abolished. |
| T6 |
536-679 |
Sentence |
denotes |
The adhesin agglutinated rabbit erythrocytes but when the latter were desialylated or pronase treated the agglutinating activity was abolished. |
| T6 |
536-679 |
Sentence |
denotes |
The adhesin agglutinated rabbit erythrocytes but when the latter were desialylated or pronase treated the agglutinating activity was abolished. |
| TextSentencer_T7 |
680-835 |
Sentence |
denotes |
The agglutinating activity of the adhesin was inhibited with N-acetyl-D-glucosamine (GlcNAc), and in a lesser degree with N-acetyl-neuraminic acid (NeuAc). |
| T7 |
680-835 |
Sentence |
denotes |
The agglutinating activity of the adhesin was inhibited with N-acetyl-D-glucosamine (GlcNAc), and in a lesser degree with N-acetyl-neuraminic acid (NeuAc). |
| T7 |
680-835 |
Sentence |
denotes |
The agglutinating activity of the adhesin was inhibited with N-acetyl-D-glucosamine (GlcNAc), and in a lesser degree with N-acetyl-neuraminic acid (NeuAc). |
| TextSentencer_T8 |
836-955 |
Sentence |
denotes |
GalNAc, N-glycolyl-neuraminic acid, N-deacetylated GlcNAc, or neutral sugars do not modify the activity of the adhesin. |
| T8 |
836-955 |
Sentence |
denotes |
GalNAc, N-glycolyl-neuraminic acid, N-deacetylated GlcNAc, or neutral sugars do not modify the activity of the adhesin. |
| T8 |
836-955 |
Sentence |
denotes |
GalNAc, N-glycolyl-neuraminic acid, N-deacetylated GlcNAc, or neutral sugars do not modify the activity of the adhesin. |
| TextSentencer_T9 |
956-1149 |
Sentence |
denotes |
The equatorial -OH on C4 and the NH-acetylated group on C2 from GlcNAc, as well as the 4-OH and NH-acetylated group on C5 from NeuAc seem to be responsible for the interaction with the adhesin. |
| T9 |
956-1149 |
Sentence |
denotes |
The equatorial -OH on C4 and the NH-acetylated group on C2 from GlcNAc, as well as the 4-OH and NH-acetylated group on C5 from NeuAc seem to be responsible for the interaction with the adhesin. |
| T9 |
956-1149 |
Sentence |
denotes |
The equatorial -OH on C4 and the NH-acetylated group on C2 from GlcNAc, as well as the 4-OH and NH-acetylated group on C5 from NeuAc seem to be responsible for the interaction with the adhesin. |
| TextSentencer_T10 |
1150-1208 |
Sentence |
denotes |
The protein is divalent cation-dependent and thermolabile. |
| T10 |
1150-1208 |
Sentence |
denotes |
The protein is divalent cation-dependent and thermolabile. |
| T10 |
1150-1208 |
Sentence |
denotes |
The protein is divalent cation-dependent and thermolabile. |
| TextSentencer_T11 |
1209-1444 |
Sentence |
denotes |
As for the agglutinating activity, the adhesion of P.haemolytica to tracheal cell-cultures was inhibited by GlcNAc, NeuAc or the purified adhesin, strongly suggesting that the P.haemolytica adhesin plays an important role in infection. |
| T11 |
1209-1444 |
Sentence |
denotes |
As for the agglutinating activity, the adhesion of P.haemolytica to tracheal cell-cultures was inhibited by GlcNAc, NeuAc or the purified adhesin, strongly suggesting that the P.haemolytica adhesin plays an important role in infection. |
| T11 |
1209-1444 |
Sentence |
denotes |
As for the agglutinating activity, the adhesion of P.haemolytica to tracheal cell-cultures was inhibited by GlcNAc, NeuAc or the purified adhesin, strongly suggesting that the P.haemolytica adhesin plays an important role in infection. |