| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-99 |
Sentence |
denotes |
Purification and characterization of a smooth muscle myosin light chain kinase-phosphatase complex. |
| T2 |
100-260 |
Sentence |
denotes |
We show that a myofibrillar form of smooth muscle myosin light chain phosphatase (MLCPase) forms a multienzyme complex with myosin light chain kinase (MLCKase). |
| T3 |
261-625 |
Sentence |
denotes |
The stability of the complex was indicated by the copurification of MLCKase and MLCPase activities through multiple steps that included myofibril preparation, gel filtration chromatography, cation (SP-Sepharose BB) and anion (Q-Sepharose FF) exchange chromatography, and affinity purification on calmodulin and on thiophosphorylated regulatory light chain columns. |
| T4 |
626-755 |
Sentence |
denotes |
In addition, the purified complex eluted as a single peak from a final gel filtration column in the presence of calmodulin (CaM). |
| T5 |
756-955 |
Sentence |
denotes |
Because a similar MLCPase is present in varying amounts in standard preparations of both MLCKase and myosin filaments, we have named it a kinase- and myosin-associated protein phosphatase (KAMPPase). |
| T6 |
956-1103 |
Sentence |
denotes |
The KAMPPase multienzyme complex was composed of a 37-kDa catalytic (PC) subunit, a 67-kDa targeting (PT) subunit, and MLCKase with or without CaM. |
| T7 |
1104-1226 |
Sentence |
denotes |
The approximate molar ratio of the PC and PT subunits was 1:2 with a variable and usually higher molar content of MLCKase. |
| T8 |
1227-1373 |
Sentence |
denotes |
The targeting role of the PT subunit was directly demonstrated in binding experiments in which the PT subunit bound to both the kinase and to CaM. |
| T9 |
1374-1424 |
Sentence |
denotes |
Its binding to CaM was, however, Ca2+-independent. |
| T10 |
1425-1536 |
Sentence |
denotes |
MLCKase and the PT subunit potentiated activity of the PC subunit when intact myosin was used as the substrate. |
| T11 |
1537-1699 |
Sentence |
denotes |
These data indicated that there is a Ca2+-independent interaction among the MLCPase, MLCKase, and CaM that are involved in the regulation of phosphatase activity. |
| T1 |
0-99 |
Sentence |
denotes |
Purification and characterization of a smooth muscle myosin light chain kinase-phosphatase complex. |
| T2 |
100-260 |
Sentence |
denotes |
We show that a myofibrillar form of smooth muscle myosin light chain phosphatase (MLCPase) forms a multienzyme complex with myosin light chain kinase (MLCKase). |
| T3 |
261-625 |
Sentence |
denotes |
The stability of the complex was indicated by the copurification of MLCKase and MLCPase activities through multiple steps that included myofibril preparation, gel filtration chromatography, cation (SP-Sepharose BB) and anion (Q-Sepharose FF) exchange chromatography, and affinity purification on calmodulin and on thiophosphorylated regulatory light chain columns. |
| T4 |
626-755 |
Sentence |
denotes |
In addition, the purified complex eluted as a single peak from a final gel filtration column in the presence of calmodulin (CaM). |
| T5 |
756-955 |
Sentence |
denotes |
Because a similar MLCPase is present in varying amounts in standard preparations of both MLCKase and myosin filaments, we have named it a kinase- and myosin-associated protein phosphatase (KAMPPase). |
| T6 |
956-1103 |
Sentence |
denotes |
The KAMPPase multienzyme complex was composed of a 37-kDa catalytic (PC) subunit, a 67-kDa targeting (PT) subunit, and MLCKase with or without CaM. |
| T7 |
1104-1226 |
Sentence |
denotes |
The approximate molar ratio of the PC and PT subunits was 1:2 with a variable and usually higher molar content of MLCKase. |
| T8 |
1227-1373 |
Sentence |
denotes |
The targeting role of the PT subunit was directly demonstrated in binding experiments in which the PT subunit bound to both the kinase and to CaM. |
| T9 |
1374-1424 |
Sentence |
denotes |
Its binding to CaM was, however, Ca2+-independent. |
| T10 |
1425-1536 |
Sentence |
denotes |
MLCKase and the PT subunit potentiated activity of the PC subunit when intact myosin was used as the substrate. |
| T11 |
1537-1699 |
Sentence |
denotes |
These data indicated that there is a Ca2+-independent interaction among the MLCPase, MLCKase, and CaM that are involved in the regulation of phosphatase activity. |