| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-77 |
Sentence |
denotes |
Purification and characterization of smooth muscle myosin light chain kinase. |
| T2 |
78-152 |
Sentence |
denotes |
Smooth muscle myosin light chain kinase was purified from turkey gizzards. |
| T3 |
153-305 |
Sentence |
denotes |
The enzyme was extracted from washed myofibrils and the final step of purification was affinity chromatography using calmodulin coupled to Sepharose 4B. |
| T4 |
306-407 |
Sentence |
denotes |
The purified enzyme was characterized with respect to its physical, chemical, and kinetic properties. |
| T5 |
408-593 |
Sentence |
denotes |
It has a molecular weight of 130,000 by sodium dodecyl sulfate polyacrylamide gel electrophoresis and 124,000 by sedimentation equilibrium centrifugation under nondenaturing conditions. |
| T6 |
594-729 |
Sentence |
denotes |
It is an asymmetric molecule with a Stokes radius of 75 A, a sedimentation coefficient of 4.45 S, and a frictional coefficient of 1.85. |
| T7 |
730-838 |
Sentence |
denotes |
Smooth muscle myosin light chain kinase is dependent on the calcium-binding protein calmodulin for activity. |
| T8 |
839-968 |
Sentence |
denotes |
It has an apparent K0.5 for calmodulin of 10(-9) M and binds 1 mol of calmodulin/mol of myosin kinase in the presence of calcium. |
| T9 |
969-1145 |
Sentence |
denotes |
The binding of calmodulin increases the sedimentation coefficient from 4.45 S to 5.05 S, and the Stokes radius from 75 A to 79 A, and does not alter the frictional coefficient. |
| T10 |
1146-1272 |
Sentence |
denotes |
The enzyme has a Km for ATP and the 20,000-dalton light chain of smooth muscle myosin of 50 microM and 5 microM, respectively. |
| T11 |
1273-1424 |
Sentence |
denotes |
It phosphorylates the 20,000-dalton light chain of smooth muscle myosin more rapidly than the equivalent light chain from cardiac and skeletal muscles. |
| T12 |
1425-1538 |
Sentence |
denotes |
It does not phosphorylate histones, alpha-casein, phosphorylase kinase, or phosphorylase b at a significant rate. |
| T1 |
0-77 |
Sentence |
denotes |
Purification and characterization of smooth muscle myosin light chain kinase. |
| T2 |
78-152 |
Sentence |
denotes |
Smooth muscle myosin light chain kinase was purified from turkey gizzards. |
| T3 |
153-305 |
Sentence |
denotes |
The enzyme was extracted from washed myofibrils and the final step of purification was affinity chromatography using calmodulin coupled to Sepharose 4B. |
| T4 |
306-407 |
Sentence |
denotes |
The purified enzyme was characterized with respect to its physical, chemical, and kinetic properties. |
| T5 |
408-593 |
Sentence |
denotes |
It has a molecular weight of 130,000 by sodium dodecyl sulfate polyacrylamide gel electrophoresis and 124,000 by sedimentation equilibrium centrifugation under nondenaturing conditions. |
| T6 |
594-729 |
Sentence |
denotes |
It is an asymmetric molecule with a Stokes radius of 75 A, a sedimentation coefficient of 4.45 S, and a frictional coefficient of 1.85. |
| T7 |
730-838 |
Sentence |
denotes |
Smooth muscle myosin light chain kinase is dependent on the calcium-binding protein calmodulin for activity. |
| T8 |
839-968 |
Sentence |
denotes |
It has an apparent K0.5 for calmodulin of 10(-9) M and binds 1 mol of calmodulin/mol of myosin kinase in the presence of calcium. |
| T9 |
969-1145 |
Sentence |
denotes |
The binding of calmodulin increases the sedimentation coefficient from 4.45 S to 5.05 S, and the Stokes radius from 75 A to 79 A, and does not alter the frictional coefficient. |
| T10 |
1146-1272 |
Sentence |
denotes |
The enzyme has a Km for ATP and the 20,000-dalton light chain of smooth muscle myosin of 50 microM and 5 microM, respectively. |
| T11 |
1273-1424 |
Sentence |
denotes |
It phosphorylates the 20,000-dalton light chain of smooth muscle myosin more rapidly than the equivalent light chain from cardiac and skeletal muscles. |
| T12 |
1425-1538 |
Sentence |
denotes |
It does not phosphorylate histones, alpha-casein, phosphorylase kinase, or phosphorylase b at a significant rate. |