PubMed:3131322
Annnotations
GlyCosmos6-Glycan-Motif-Image
| Id | Subject | Object | Predicate | Lexical cue | image |
|---|---|---|---|---|---|
| T1 | 2550-2558 | Glycan_Motif | denotes | F1 alpha | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G61730RY|https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G21312EA |
sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 0-120 | Sentence | denotes | Kinetic analysis of the Ca2+-dependent, membrane-bound, macrophage phospholipase A2 and the effects of arachidonic acid. |
| T2 | 121-349 | Sentence | denotes | The kinetics of the Ca2+-dependent, alkaline pH optimum, membrane-bound phospholipase A2 from the P388D1 macrophage-like cell line were studied using various phosphatidylcholine (PC) and phosphatidylethanolamine (PE) substrates. |
| T3 | 350-529 | Sentence | denotes | This enzyme exhibits "surface dilution kinetics" toward PC in Triton X-100 mixed micelles, and the "dual phospholipid model" was found to adequately describe its kinetic behavior. |
| T4 | 530-659 | Sentence | denotes | With substrate in the form of sonicated vesicles, the dual phospholipid model should give rise to Michaelis-Menten type kinetics. |
| T5 | 660-804 | Sentence | denotes | However, the hydrolysis of dipalmitoyl-PC, 1-palmitoyl-2-oleoyl-PC, and 1-stearoyl-2-arachidonoyl-PC vesicles exhibited two distinct activities. |
| T6 | 805-984 | Sentence | denotes | Below 10 microM, the data appeared to follow Michaelis-Menten behavior, while at higher concentrations, the data could best be fit to a Hill equation with a Hill coefficient of 2. |
| T7 | 985-1108 | Sentence | denotes | These PCs had Vmax values for the low substrate concentration range of 0.2-0.6 nmol min-1 mg-1 and Km values of 1-2 microM. |
| T8 | 1109-1205 | Sentence | denotes | At the high substrate concentration range, the Vmax values were between 5 and 7 nmol min-1 mg-1. |
| T9 | 1206-1374 | Sentence | denotes | PC containing unsaturated fatty acids had an apparent Km, determined from the Hill equation, of about 15 microM, while the apparent Km of dipalmitoyl-PC was 0.6 microM. |
| T10 | 1375-1523 | Sentence | denotes | When 70% glycerol was included in the assays, a single Michaelis-Menten curve was obtained for both dipalmitoyl-PC and 1-stearoyl,2-arachidonoyl-PC. |
| T11 | 1524-1723 | Sentence | denotes | Possible explanations for these kinetic results include reconstitution of the membrane-bound phospholipase A2 in the phospholipid vesicle or the enzyme has tow distinct phospholipid binding function. |
| T12 | 1724-1912 | Sentence | denotes | The kinetics for both dipalmitoyl-PC and dipalmitoyl-PE hydrolysis in vesicles was very similar, indicating that the enzyme does not greatly prefer one of these head groups over the other. |
| T13 | 1913-1991 | Sentence | denotes | The enzyme also showed no preference for arachidonoyl containing phospholipid. |
| T14 | 1992-2179 | Sentence | denotes | Enzymatic activity toward PC containing saturated fatty acids was linear to about 15% hydrolysis while the hydrolysis of PC containing unsaturated fatty acids was linear to only about 5%. |
| T15 | 2180-2261 | Sentence | denotes | This loss of linearity was due to inhibition by released unsaturated fatty acids. |
| T16 | 2262-2370 | Sentence | denotes | Arachidonic acid was found to be a competitive inhibitor of dipalmitoyl PC hydrolysis with a K1 of 5 microM. |
| T17 | 2371-2455 | Sentence | denotes | This tight binding suggests a possible in vivo regulatory role for arachidonic acid. |
| T18 | 2456-2623 | Sentence | denotes | Three compounds of the arachidonic acid cascade, prostaglandin F2 alpha, 6-keto-prostaglandin F1 alpha, and thromboxane B2, showed no inhibition of enzymatic activity. |
| T1 | 0-120 | Sentence | denotes | Kinetic analysis of the Ca2+-dependent, membrane-bound, macrophage phospholipase A2 and the effects of arachidonic acid. |
| T2 | 121-349 | Sentence | denotes | The kinetics of the Ca2+-dependent, alkaline pH optimum, membrane-bound phospholipase A2 from the P388D1 macrophage-like cell line were studied using various phosphatidylcholine (PC) and phosphatidylethanolamine (PE) substrates. |
| T3 | 350-529 | Sentence | denotes | This enzyme exhibits "surface dilution kinetics" toward PC in Triton X-100 mixed micelles, and the "dual phospholipid model" was found to adequately describe its kinetic behavior. |
| T4 | 530-659 | Sentence | denotes | With substrate in the form of sonicated vesicles, the dual phospholipid model should give rise to Michaelis-Menten type kinetics. |
| T5 | 660-804 | Sentence | denotes | However, the hydrolysis of dipalmitoyl-PC, 1-palmitoyl-2-oleoyl-PC, and 1-stearoyl-2-arachidonoyl-PC vesicles exhibited two distinct activities. |
| T6 | 805-984 | Sentence | denotes | Below 10 microM, the data appeared to follow Michaelis-Menten behavior, while at higher concentrations, the data could best be fit to a Hill equation with a Hill coefficient of 2. |
| T7 | 985-1108 | Sentence | denotes | These PCs had Vmax values for the low substrate concentration range of 0.2-0.6 nmol min-1 mg-1 and Km values of 1-2 microM. |
| T8 | 1109-1205 | Sentence | denotes | At the high substrate concentration range, the Vmax values were between 5 and 7 nmol min-1 mg-1. |
| T9 | 1206-1374 | Sentence | denotes | PC containing unsaturated fatty acids had an apparent Km, determined from the Hill equation, of about 15 microM, while the apparent Km of dipalmitoyl-PC was 0.6 microM. |
| T10 | 1375-1523 | Sentence | denotes | When 70% glycerol was included in the assays, a single Michaelis-Menten curve was obtained for both dipalmitoyl-PC and 1-stearoyl,2-arachidonoyl-PC. |
| T11 | 1524-1723 | Sentence | denotes | Possible explanations for these kinetic results include reconstitution of the membrane-bound phospholipase A2 in the phospholipid vesicle or the enzyme has tow distinct phospholipid binding function. |
| T12 | 1724-1912 | Sentence | denotes | The kinetics for both dipalmitoyl-PC and dipalmitoyl-PE hydrolysis in vesicles was very similar, indicating that the enzyme does not greatly prefer one of these head groups over the other. |
| T13 | 1913-1991 | Sentence | denotes | The enzyme also showed no preference for arachidonoyl containing phospholipid. |
| T14 | 1992-2179 | Sentence | denotes | Enzymatic activity toward PC containing saturated fatty acids was linear to about 15% hydrolysis while the hydrolysis of PC containing unsaturated fatty acids was linear to only about 5%. |
| T15 | 2180-2261 | Sentence | denotes | This loss of linearity was due to inhibition by released unsaturated fatty acids. |
| T16 | 2262-2370 | Sentence | denotes | Arachidonic acid was found to be a competitive inhibitor of dipalmitoyl PC hydrolysis with a K1 of 5 microM. |
| T17 | 2371-2455 | Sentence | denotes | This tight binding suggests a possible in vivo regulatory role for arachidonic acid. |
| T18 | 2456-2623 | Sentence | denotes | Three compounds of the arachidonic acid cascade, prostaglandin F2 alpha, 6-keto-prostaglandin F1 alpha, and thromboxane B2, showed no inhibition of enzymatic activity. |
GlyCosmos6-Glycan-Motif-Structure
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 2550-2558 | https://glytoucan.org/Structures/Glycans/G21312EA | denotes | F1 alpha |
| T2 | 2550-2558 | https://glytoucan.org/Structures/Glycans/G61730RY | denotes | F1 alpha |
Glycosmos6-GlycoEpitope
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 2550-2558 | http://www.glycoepitope.jp/epitopes/EP0024 | denotes | F1 alpha |
Glycosmos6-MAT
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 1885-1889 | http://purl.obolibrary.org/obo/MAT_0000294 | denotes | head |
GlyCosmos15-Glycan
| Id | Subject | Object | Predicate | Lexical cue | image |
|---|---|---|---|---|---|
| T1 | 2550-2558 | Glycan | denotes | F1 alpha | https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY |
mondo_disease
| Id | Subject | Object | Predicate | Lexical cue | mondo_id |
|---|---|---|---|---|---|
| T1 | 699-704 | Disease | denotes | PC, 1 | http://purl.obolibrary.org/obo/MONDO_0008173 |
Anatomy-MAT
| Id | Subject | Object | Predicate | Lexical cue | mat_id |
|---|---|---|---|---|---|
| T1 | 1885-1889 | Body_part | denotes | head | http://purl.obolibrary.org/obo/MAT_0000294 |
Glycan-GlyCosmos
| Id | Subject | Object | Predicate | Lexical cue | image |
|---|---|---|---|---|---|
| T1 | 2550-2558 | Glycan | denotes | F1 alpha | https://api.glycosmos.org/wurcs2image/latest/png/binary/G61730RY |
GlyCosmos-GlycoEpitope
| Id | Subject | Object | Predicate | Lexical cue | glycoepitope_id |
|---|---|---|---|---|---|
| T1 | 2550-2558 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | F1 alpha | http://www.glycoepitope.jp/epitopes/EP0024 |
GlyCosmos15-CL
| Id | Subject | Object | Predicate | Lexical cue | cl_id |
|---|---|---|---|---|---|
| T1 | 56-66 | Cell | denotes | macrophage | http://purl.obolibrary.org/obo/CL:0000235|http://purl.obolibrary.org/obo/CL:0000394 |
| T3 | 226-236 | Cell | denotes | macrophage | http://purl.obolibrary.org/obo/CL:0000235|http://purl.obolibrary.org/obo/CL:0000394 |
GlyCosmos15-Sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 0-120 | Sentence | denotes | Kinetic analysis of the Ca2+-dependent, membrane-bound, macrophage phospholipase A2 and the effects of arachidonic acid. |
| T2 | 121-349 | Sentence | denotes | The kinetics of the Ca2+-dependent, alkaline pH optimum, membrane-bound phospholipase A2 from the P388D1 macrophage-like cell line were studied using various phosphatidylcholine (PC) and phosphatidylethanolamine (PE) substrates. |
| T3 | 350-529 | Sentence | denotes | This enzyme exhibits "surface dilution kinetics" toward PC in Triton X-100 mixed micelles, and the "dual phospholipid model" was found to adequately describe its kinetic behavior. |
| T4 | 530-659 | Sentence | denotes | With substrate in the form of sonicated vesicles, the dual phospholipid model should give rise to Michaelis-Menten type kinetics. |
| T5 | 660-804 | Sentence | denotes | However, the hydrolysis of dipalmitoyl-PC, 1-palmitoyl-2-oleoyl-PC, and 1-stearoyl-2-arachidonoyl-PC vesicles exhibited two distinct activities. |
| T6 | 805-984 | Sentence | denotes | Below 10 microM, the data appeared to follow Michaelis-Menten behavior, while at higher concentrations, the data could best be fit to a Hill equation with a Hill coefficient of 2. |
| T7 | 985-1108 | Sentence | denotes | These PCs had Vmax values for the low substrate concentration range of 0.2-0.6 nmol min-1 mg-1 and Km values of 1-2 microM. |
| T8 | 1109-1205 | Sentence | denotes | At the high substrate concentration range, the Vmax values were between 5 and 7 nmol min-1 mg-1. |
| T9 | 1206-1374 | Sentence | denotes | PC containing unsaturated fatty acids had an apparent Km, determined from the Hill equation, of about 15 microM, while the apparent Km of dipalmitoyl-PC was 0.6 microM. |
| T10 | 1375-1523 | Sentence | denotes | When 70% glycerol was included in the assays, a single Michaelis-Menten curve was obtained for both dipalmitoyl-PC and 1-stearoyl,2-arachidonoyl-PC. |
| T11 | 1524-1723 | Sentence | denotes | Possible explanations for these kinetic results include reconstitution of the membrane-bound phospholipase A2 in the phospholipid vesicle or the enzyme has tow distinct phospholipid binding function. |
| T12 | 1724-1912 | Sentence | denotes | The kinetics for both dipalmitoyl-PC and dipalmitoyl-PE hydrolysis in vesicles was very similar, indicating that the enzyme does not greatly prefer one of these head groups over the other. |
| T13 | 1913-1991 | Sentence | denotes | The enzyme also showed no preference for arachidonoyl containing phospholipid. |
| T14 | 1992-2179 | Sentence | denotes | Enzymatic activity toward PC containing saturated fatty acids was linear to about 15% hydrolysis while the hydrolysis of PC containing unsaturated fatty acids was linear to only about 5%. |
| T15 | 2180-2261 | Sentence | denotes | This loss of linearity was due to inhibition by released unsaturated fatty acids. |
| T16 | 2262-2370 | Sentence | denotes | Arachidonic acid was found to be a competitive inhibitor of dipalmitoyl PC hydrolysis with a K1 of 5 microM. |
| T17 | 2371-2455 | Sentence | denotes | This tight binding suggests a possible in vivo regulatory role for arachidonic acid. |
| T18 | 2456-2623 | Sentence | denotes | Three compounds of the arachidonic acid cascade, prostaglandin F2 alpha, 6-keto-prostaglandin F1 alpha, and thromboxane B2, showed no inhibition of enzymatic activity. |
GlyCosmos15-GlycoEpitope
| Id | Subject | Object | Predicate | Lexical cue | glycoepitope_id |
|---|---|---|---|---|---|
| T1 | 2550-2558 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | F1 alpha | http://www.glycoepitope.jp/epitopes/EP0024 |
GlyCosmos15-UBERON
| Id | Subject | Object | Predicate | Lexical cue | uberon_id |
|---|---|---|---|---|---|
| T1 | 40-48 | Body_part | denotes | membrane | http://purl.obolibrary.org/obo/UBERON_0000094 |
| T2 | 56-66 | Body_part | denotes | macrophage | http://purl.obolibrary.org/obo/CL_0000235 |
| T3 | 178-186 | Body_part | denotes | membrane | http://purl.obolibrary.org/obo/UBERON_0000094 |
| T4 | 226-236 | Body_part | denotes | macrophage | http://purl.obolibrary.org/obo/CL_0000235 |
| T5 | 1602-1610 | Body_part | denotes | membrane | http://purl.obolibrary.org/obo/UBERON_0000094 |
| T6 | 1654-1661 | Body_part | denotes | vesicle | http://purl.obolibrary.org/obo/GO_0031982 |
| T7 | 1885-1889 | Body_part | denotes | head | http://purl.obolibrary.org/obo/UBERON_0000033 |
GlyCosmos15-FMA
| Id | Subject | Object | Predicate | Lexical cue | db_id |
|---|---|---|---|---|---|
| T1 | 56-66 | Body_part | denotes | macrophage | FMA:63261 |
| T2 | 226-236 | Body_part | denotes | macrophage | FMA:63261 |
| T3 | 1885-1889 | Body_part | denotes | head | FMA:7154 |
GlyCosmos15-MAT
| Id | Subject | Object | Predicate | Lexical cue | mat_id |
|---|---|---|---|---|---|
| T1 | 1885-1889 | Body_part | denotes | head | http://purl.obolibrary.org/obo/MAT_0000294 |
Anatomy-UBERON
| Id | Subject | Object | Predicate | Lexical cue | uberon_id |
|---|---|---|---|---|---|
| T1 | 40-48 | Body_part | denotes | membrane | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
| T4 | 56-66 | Body_part | denotes | macrophage | http://purl.obolibrary.org/obo/CL_0000235 |
| T5 | 178-186 | Body_part | denotes | membrane | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
| T8 | 226-236 | Body_part | denotes | macrophage | http://purl.obolibrary.org/obo/CL_0000235 |
| T9 | 1602-1610 | Body_part | denotes | membrane | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
| T12 | 1654-1661 | Body_part | denotes | vesicle | http://purl.obolibrary.org/obo/GO_0031982 |
| T13 | 1885-1889 | Body_part | denotes | head | http://purl.obolibrary.org/obo/UBERON_0000033 |
CL-cell
| Id | Subject | Object | Predicate | Lexical cue | cl_id |
|---|---|---|---|---|---|
| T1 | 56-66 | Cell | denotes | macrophage | http://purl.obolibrary.org/obo/CL:0000235|http://purl.obolibrary.org/obo/CL:0000394 |
| T3 | 226-236 | Cell | denotes | macrophage | http://purl.obolibrary.org/obo/CL:0000235|http://purl.obolibrary.org/obo/CL:0000394 |