| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-87 |
Sentence |
denotes |
Isolation and characterization of a novel acetyl-CoA carboxylase kinase from rat liver. |
| T1 |
0-87 |
Sentence |
denotes |
Isolation and characterization of a novel acetyl-CoA carboxylase kinase from rat liver. |
| T2 |
88-214 |
Sentence |
denotes |
Acetyl-CoA carboxylase is regulated allosterically by citrate and covalently by a phosphorylation/dephosphorylation mechanism. |
| T2 |
88-214 |
Sentence |
denotes |
Acetyl-CoA carboxylase is regulated allosterically by citrate and covalently by a phosphorylation/dephosphorylation mechanism. |
| T3 |
215-328 |
Sentence |
denotes |
We have isolated and purified from rat livers a novel kinase that phosphorylates and inactivates the carboxylase. |
| T3 |
215-328 |
Sentence |
denotes |
We have isolated and purified from rat livers a novel kinase that phosphorylates and inactivates the carboxylase. |
| T4 |
329-409 |
Sentence |
denotes |
This kinase is bound to the carboxylase and can be eluted in salt-rich solution. |
| T4 |
329-409 |
Sentence |
denotes |
This kinase is bound to the carboxylase and can be eluted in salt-rich solution. |
| T5 |
410-522 |
Sentence |
denotes |
The native kinase exists as high molecular weight aggregates of a subunit that has a molecular weight of 40,000. |
| T5 |
410-522 |
Sentence |
denotes |
The native kinase exists as high molecular weight aggregates of a subunit that has a molecular weight of 40,000. |
| T6 |
523-726 |
Sentence |
denotes |
The phosphorylation sites of the carboxylase were determined after tryptic and cyanogen bromide digestions of 32P-labeled carboxylase and separation of the peptides by various chromatographic procedures. |
| T6 |
523-726 |
Sentence |
denotes |
The phosphorylation sites of the carboxylase were determined after tryptic and cyanogen bromide digestions of 32P-labeled carboxylase and separation of the peptides by various chromatographic procedures. |
| T7 |
727-847 |
Sentence |
denotes |
Amino acid analyses of the phosphopeptides showed that the Ser77 and Ser1200 residues were the sites of phosphorylation. |
| T7 |
727-847 |
Sentence |
denotes |
Amino acid analyses of the phosphopeptides showed that the Ser77 and Ser1200 residues were the sites of phosphorylation. |
| T8 |
848-1005 |
Sentence |
denotes |
Treating the phosphorylated carboxylase with the Mn(2+)-dependent acetyl-CoA carboxylase phosphatase 2 removed the phosphate and reactivated the carboxylase. |
| T8 |
848-1005 |
Sentence |
denotes |
Treating the phosphorylated carboxylase with the Mn(2+)-dependent acetyl-CoA carboxylase phosphatase 2 removed the phosphate and reactivated the carboxylase. |
| T9 |
1006-1158 |
Sentence |
denotes |
These results suggest that both this kinase and the acetyl-CoA carboxylase phosphatase 2 act at the same site(s) in the acetyl-CoA carboxylase molecule. |
| T9 |
1006-1158 |
Sentence |
denotes |
These results suggest that both this kinase and the acetyl-CoA carboxylase phosphatase 2 act at the same site(s) in the acetyl-CoA carboxylase molecule. |
| T10 |
1159-1424 |
Sentence |
denotes |
Citrate dramatically inhibits the kinase-mediated phosphorylation of the carboxylase, suggesting that the allosteric modification and activation by citrate render the phosphorylation sites inaccessible to the kinase and therefore maintain high carboxylase activity. |
| T10 |
1159-1424 |
Sentence |
denotes |
Citrate dramatically inhibits the kinase-mediated phosphorylation of the carboxylase, suggesting that the allosteric modification and activation by citrate render the phosphorylation sites inaccessible to the kinase and therefore maintain high carboxylase activity. |
| T11 |
1425-1580 |
Sentence |
denotes |
This observation indicates that there is a close interplay between the citrate effect on and phosphorylation of the carboxylase in regulating its activity. |
| T11 |
1425-1580 |
Sentence |
denotes |
This observation indicates that there is a close interplay between the citrate effect on and phosphorylation of the carboxylase in regulating its activity. |