> top > projects > sentences > docs > PubMed:9054394 > annotations
sentences Home  

PubMed:9054394 JSONTXT 23 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-99 Sentence denotes Purification and characterization of a smooth muscle myosin light chain kinase-phosphatase complex.
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).
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.
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).
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).
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.
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.
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.
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.
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.
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.
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.