PubMed:17602139
Annnotations
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
TextSentencer_T1 | 0-126 | Sentence | denotes | Kinetics of Hyal-1 and PH-20 hyaluronidases: comparison of minimal substrates and analysis of the transglycosylation reaction. |
TextSentencer_T2 | 127-322 | Sentence | denotes | The availability of recombinant expression systems for the production of purified human hyaluronidases PH-20 and Hyal-1 facilitated the first detailed analysis of the enzymatic reaction products. |
TextSentencer_T3 | 323-588 | Sentence | denotes | The human recombinant enzymes, both expressed by Drosophila Schneider-2 (DS-2) cells, were compared to bovine testicular hyaluronidase (BTH), a commercially available hyaluronidase preparation, which has long been considered a prototype of mammalian hyaluronidases. |
TextSentencer_T4 | 589-721 | Sentence | denotes | The conversion of low molecular weight hyaluronic acid (HA) fragments was detected by a capillary zone electrophoresis (CZE) method. |
TextSentencer_T5 | 722-881 | Sentence | denotes | Surprisingly, the HA hexasaccharide, which is generally accepted to be the minimum substrate of BTH, was not a substrate of recombinant human PH-20 and Hyal-1. |
TextSentencer_T6 | 882-1019 | Sentence | denotes | However, HA octasaccharide was converted efficiently by both enzymes, thus representing the minimum substrate for human PH-20 and Hyal-1. |
TextSentencer_T7 | 1020-1161 | Sentence | denotes | Additionally, BTH was shown to catabolize the HA hexasaccharide at pH 4.0 mainly by hydrolysis, while at pH 6.0 transglycosylation prevailed. |
TextSentencer_T8 | 1162-1260 | Sentence | denotes | Human PH-20 was found to catalyze both hydrolysis and transglycosylation of the HA octasaccharide. |
TextSentencer_T9 | 1261-1445 | Sentence | denotes | On the contrary, human Hyal-1 converted the HA octasaccharide mainly by hydrolysis with transglycosylation products occurring only at high substrate concentrations (> or = 500 microM). |
TextSentencer_T10 | 1446-1551 | Sentence | denotes | The differences between the hyaluronidase subtypes and isoenzymes were much more prominent than expected. |
TextSentencer_T11 | 1552-1695 | Sentence | denotes | Obviously, the different hyaluronidase subtypes have evolved into very specialized enzymes with respect to their catalytic mechanism of action. |
T1 | 0-126 | Sentence | denotes | Kinetics of Hyal-1 and PH-20 hyaluronidases: comparison of minimal substrates and analysis of the transglycosylation reaction. |
T2 | 127-322 | Sentence | denotes | The availability of recombinant expression systems for the production of purified human hyaluronidases PH-20 and Hyal-1 facilitated the first detailed analysis of the enzymatic reaction products. |
T3 | 323-588 | Sentence | denotes | The human recombinant enzymes, both expressed by Drosophila Schneider-2 (DS-2) cells, were compared to bovine testicular hyaluronidase (BTH), a commercially available hyaluronidase preparation, which has long been considered a prototype of mammalian hyaluronidases. |
T4 | 589-721 | Sentence | denotes | The conversion of low molecular weight hyaluronic acid (HA) fragments was detected by a capillary zone electrophoresis (CZE) method. |
T5 | 722-881 | Sentence | denotes | Surprisingly, the HA hexasaccharide, which is generally accepted to be the minimum substrate of BTH, was not a substrate of recombinant human PH-20 and Hyal-1. |
T6 | 882-1019 | Sentence | denotes | However, HA octasaccharide was converted efficiently by both enzymes, thus representing the minimum substrate for human PH-20 and Hyal-1. |
T7 | 1020-1161 | Sentence | denotes | Additionally, BTH was shown to catabolize the HA hexasaccharide at pH 4.0 mainly by hydrolysis, while at pH 6.0 transglycosylation prevailed. |
T8 | 1162-1260 | Sentence | denotes | Human PH-20 was found to catalyze both hydrolysis and transglycosylation of the HA octasaccharide. |
T9 | 1261-1445 | Sentence | denotes | On the contrary, human Hyal-1 converted the HA octasaccharide mainly by hydrolysis with transglycosylation products occurring only at high substrate concentrations (> or = 500 microM). |
T10 | 1446-1551 | Sentence | denotes | The differences between the hyaluronidase subtypes and isoenzymes were much more prominent than expected. |
T11 | 1552-1695 | Sentence | denotes | Obviously, the different hyaluronidase subtypes have evolved into very specialized enzymes with respect to their catalytic mechanism of action. |
T1 | 0-126 | Sentence | denotes | Kinetics of Hyal-1 and PH-20 hyaluronidases: comparison of minimal substrates and analysis of the transglycosylation reaction. |
T2 | 127-322 | Sentence | denotes | The availability of recombinant expression systems for the production of purified human hyaluronidases PH-20 and Hyal-1 facilitated the first detailed analysis of the enzymatic reaction products. |
T3 | 323-588 | Sentence | denotes | The human recombinant enzymes, both expressed by Drosophila Schneider-2 (DS-2) cells, were compared to bovine testicular hyaluronidase (BTH), a commercially available hyaluronidase preparation, which has long been considered a prototype of mammalian hyaluronidases. |
T4 | 589-721 | Sentence | denotes | The conversion of low molecular weight hyaluronic acid (HA) fragments was detected by a capillary zone electrophoresis (CZE) method. |
T5 | 722-881 | Sentence | denotes | Surprisingly, the HA hexasaccharide, which is generally accepted to be the minimum substrate of BTH, was not a substrate of recombinant human PH-20 and Hyal-1. |
T6 | 882-1019 | Sentence | denotes | However, HA octasaccharide was converted efficiently by both enzymes, thus representing the minimum substrate for human PH-20 and Hyal-1. |
T7 | 1020-1161 | Sentence | denotes | Additionally, BTH was shown to catabolize the HA hexasaccharide at pH 4.0 mainly by hydrolysis, while at pH 6.0 transglycosylation prevailed. |
T8 | 1162-1260 | Sentence | denotes | Human PH-20 was found to catalyze both hydrolysis and transglycosylation of the HA octasaccharide. |
T9 | 1261-1445 | Sentence | denotes | On the contrary, human Hyal-1 converted the HA octasaccharide mainly by hydrolysis with transglycosylation products occurring only at high substrate concentrations (> or = 500 microM). |
T10 | 1446-1551 | Sentence | denotes | The differences between the hyaluronidase subtypes and isoenzymes were much more prominent than expected. |
T11 | 1552-1695 | Sentence | denotes | Obviously, the different hyaluronidase subtypes have evolved into very specialized enzymes with respect to their catalytic mechanism of action. |
uniprot-human
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 12-18 | http://www.uniprot.org/uniprot/Q8NFK8 | denotes | Hyal-1 |
T2 | 240-246 | http://www.uniprot.org/uniprot/Q8NFK8 | denotes | Hyal-1 |
T3 | 874-880 | http://www.uniprot.org/uniprot/Q8NFK8 | denotes | Hyal-1 |
T4 | 1012-1018 | http://www.uniprot.org/uniprot/Q8NFK8 | denotes | Hyal-1 |
T5 | 1284-1290 | http://www.uniprot.org/uniprot/Q8NFK8 | denotes | Hyal-1 |
T6 | 23-25 | http://www.uniprot.org/uniprot/P01298 | denotes | PH |
T7 | 230-232 | http://www.uniprot.org/uniprot/P01298 | denotes | PH |
T8 | 864-866 | http://www.uniprot.org/uniprot/P01298 | denotes | PH |
T9 | 1002-1004 | http://www.uniprot.org/uniprot/P01298 | denotes | PH |
T10 | 1168-1170 | http://www.uniprot.org/uniprot/P01298 | denotes | PH |
T11 | 23-43 | http://www.uniprot.org/uniprot/P38567 | denotes | PH-20 hyaluronidases |
T12 | 215-235 | http://www.uniprot.org/uniprot/P38567 | denotes | hyaluronidases PH-20 |
T13 | 396-398 | http://www.uniprot.org/uniprot/P49366 | denotes | DS |
T14 | 645-647 | http://www.uniprot.org/uniprot/P69208 | denotes | HA |
T15 | 740-742 | http://www.uniprot.org/uniprot/P69208 | denotes | HA |
T16 | 891-893 | http://www.uniprot.org/uniprot/P69208 | denotes | HA |
T17 | 1066-1068 | http://www.uniprot.org/uniprot/P69208 | denotes | HA |
T18 | 1242-1244 | http://www.uniprot.org/uniprot/P69208 | denotes | HA |
T19 | 1305-1307 | http://www.uniprot.org/uniprot/P69208 | denotes | HA |
uniprot-mouse
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 12-18 | http://www.uniprot.org/uniprot/Q91ZJ9 | denotes | Hyal-1 |
T2 | 240-246 | http://www.uniprot.org/uniprot/Q91ZJ9 | denotes | Hyal-1 |
T3 | 874-880 | http://www.uniprot.org/uniprot/Q91ZJ9 | denotes | Hyal-1 |
T4 | 1012-1018 | http://www.uniprot.org/uniprot/Q91ZJ9 | denotes | Hyal-1 |
T5 | 1284-1290 | http://www.uniprot.org/uniprot/Q91ZJ9 | denotes | Hyal-1 |
T6 | 23-25 | http://www.uniprot.org/uniprot/P10601 | denotes | PH |
T7 | 230-232 | http://www.uniprot.org/uniprot/P10601 | denotes | PH |
T8 | 864-866 | http://www.uniprot.org/uniprot/P10601 | denotes | PH |
T9 | 1002-1004 | http://www.uniprot.org/uniprot/P10601 | denotes | PH |
T10 | 1168-1170 | http://www.uniprot.org/uniprot/P10601 | denotes | PH |
T11 | 23-43 | http://www.uniprot.org/uniprot/P48794 | denotes | PH-20 hyaluronidases |
T12 | 215-235 | http://www.uniprot.org/uniprot/P48794 | denotes | hyaluronidases PH-20 |
GlycoBiology-NCBITAXON
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 12-16 | http://purl.bioontology.org/ontology/NCBITAXON/199485 | denotes | Hyal |
T2 | 240-244 | http://purl.bioontology.org/ontology/NCBITAXON/199485 | denotes | Hyal |
T3 | 372-382 | http://purl.bioontology.org/ontology/NCBITAXON/48321 | denotes | Drosophila |
T4 | 372-382 | http://purl.bioontology.org/ontology/NCBITAXON/186285 | denotes | Drosophila |
T5 | 372-382 | http://purl.bioontology.org/ontology/NCBITAXON/32281 | denotes | Drosophila |
T6 | 372-382 | http://purl.bioontology.org/ontology/NCBITAXON/7215 | denotes | Drosophila |
T7 | 372-382 | http://purl.bioontology.org/ontology/NCBITAXON/937257 | denotes | Drosophila |
T8 | 372-382 | http://purl.bioontology.org/ontology/NCBITAXON/30026 | denotes | Drosophila |
T9 | 372-382 | http://purl.bioontology.org/ontology/NCBITAXON/46879 | denotes | Drosophila |
T10 | 372-382 | http://purl.bioontology.org/ontology/NCBITAXON/43845 | denotes | Drosophila |
T11 | 372-382 | http://purl.bioontology.org/ontology/NCBITAXON/463113 | denotes | Drosophila |
T12 | 372-382 | http://purl.bioontology.org/ontology/NCBITAXON/1226646 | denotes | Drosophila |
T13 | 372-382 | http://purl.bioontology.org/ontology/NCBITAXON/937324 | denotes | Drosophila |
T14 | 372-382 | http://purl.bioontology.org/ontology/NCBITAXON/7214 | denotes | Drosophila |
T15 | 372-382 | http://purl.bioontology.org/ontology/NCBITAXON/348021 | denotes | Drosophila |
T16 | 402-407 | http://purl.bioontology.org/ontology/STY/T025 | denotes | cells |
T17 | 677-686 | http://purl.bioontology.org/ontology/NCBITAXON/119095 | denotes | capillary |
T18 | 677-686 | http://purl.bioontology.org/ontology/NCBITAXON/241203 | denotes | capillary |
T19 | 874-878 | http://purl.bioontology.org/ontology/NCBITAXON/199485 | denotes | Hyal |
T20 | 1012-1016 | http://purl.bioontology.org/ontology/NCBITAXON/199485 | denotes | Hyal |
T21 | 1284-1288 | http://purl.bioontology.org/ontology/NCBITAXON/199485 | denotes | Hyal |
T22 | 1675-1684 | http://purl.bioontology.org/ontology/NCBITAXON/127244 | denotes | mechanism |
GO-BP
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 1051-1061 | http://purl.obolibrary.org/obo/GO_0009056 | denotes | catabolize |
GO-CC
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 402-407 | http://purl.obolibrary.org/obo/GO_0005623 | denotes | cells |
UBERON-AE
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 12-16 | http://purl.obolibrary.org/obo/UBERON_3000101 | denotes | Hyal |
T2 | 240-244 | http://purl.obolibrary.org/obo/UBERON_3000101 | denotes | Hyal |
T3 | 874-878 | http://purl.obolibrary.org/obo/UBERON_3000101 | denotes | Hyal |
T4 | 1012-1016 | http://purl.obolibrary.org/obo/UBERON_3000101 | denotes | Hyal |
T5 | 1284-1288 | http://purl.obolibrary.org/obo/UBERON_3000101 | denotes | Hyal |
T6 | 677-686 | http://purl.obolibrary.org/obo/UBERON_0001982 | denotes | capillary |
performance-test
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
PD-UBERON-AE-B_T1 | 12-16 | http://purl.obolibrary.org/obo/UBERON_3000101 | denotes | Hyal |
PD-UBERON-AE-B_T2 | 240-244 | http://purl.obolibrary.org/obo/UBERON_3000101 | denotes | Hyal |
PD-UBERON-AE-B_T3 | 874-878 | http://purl.obolibrary.org/obo/UBERON_3000101 | denotes | Hyal |
PD-UBERON-AE-B_T4 | 1012-1016 | http://purl.obolibrary.org/obo/UBERON_3000101 | denotes | Hyal |
PD-UBERON-AE-B_T5 | 1284-1288 | http://purl.obolibrary.org/obo/UBERON_3000101 | denotes | Hyal |
PD-UBERON-AE-B_T6 | 677-686 | http://purl.obolibrary.org/obo/UBERON_0001982 | denotes | capillary |
NCBITAXON
Id | Subject | Object | Predicate | Lexical cue | db_id |
---|---|---|---|---|---|
T1 | 209-214 | OrganismTaxon | denotes | human | 9606 |
T2 | 327-332 | OrganismTaxon | denotes | human | 9606 |
T3 | 372-382 | OrganismTaxon | denotes | Drosophila | 2081351|32281|7215 |
T6 | 426-432 | OrganismTaxon | denotes | bovine | 9913 |
T7 | 858-863 | OrganismTaxon | denotes | human | 9606 |
T8 | 996-1001 | OrganismTaxon | denotes | human | 9606 |
T9 | 1162-1167 | OrganismTaxon | denotes | Human | 9606 |
T10 | 1278-1283 | OrganismTaxon | denotes | human | 9606 |
T11 | 1527-1536 | OrganismTaxon | denotes | prominent | 37571 |
Anatomy-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 677-686 | Body_part | denotes | capillary | http://purl.obolibrary.org/obo/UBERON_0001982 |