| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-110 |
Sentence |
denotes |
Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase. |
| T2 |
111-238 |
Sentence |
denotes |
Limited proteolysis has been utilized to study the structural organization of rabbit skeletal muscle myosin light chain kinase. |
| T3 |
239-555 |
Sentence |
denotes |
The enzyme (Mr approximately 89,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis) consists of an amino-terminal, protease-susceptible region of unidentified function and a carboxyl-terminal, protease-resistant region of Mr approximately 40,000 containing the catalytic and calmodulin-binding domains. |
| T4 |
556-737 |
Sentence |
denotes |
Partial digestion with trypsin produced an intermediate 56,000-dalton fragment and a stable 38,000-dalton fragment, both of which were catalytically active and calmodulin-dependent. |
| T5 |
738-850 |
Sentence |
denotes |
Chymotryptic digestion yielded three catalytically active fragments of about 37,000, 36,000, and 35,000 daltons. |
| T6 |
851-988 |
Sentence |
denotes |
The Mr = 37,000 fragment was calmodulin-dependent with an apparent affinity equivalent to that of the native enzyme (approximately 1 nM). |
| T7 |
989-1103 |
Sentence |
denotes |
The 36,000-dalton fragment was also calmodulin-dependent but had a approximately 200-fold lower apparent affinity. |
| T8 |
1104-1156 |
Sentence |
denotes |
The Mr = 35,000 fragment was calmodulin-independent. |
| T9 |
1157-1221 |
Sentence |
denotes |
These three chymotryptic fragments, had identical amino termini. |
| T10 |
1222-1440 |
Sentence |
denotes |
Nineteen residues were missing from the carboxyl terminus of the calmodulin-independent chymotryptic fragment whereas only 8 or 9 carboxyl-terminal residues were missing from the calmodulin-dependent tryptic fragments. |
| T11 |
1441-1617 |
Sentence |
denotes |
These results suggest that the 11-residue sequence (IAVSAANRFKK) in the carboxyl-terminal region of myosin light chain kinase contributes directly to the binding of calmodulin. |
| T12 |
1618-1672 |
Sentence |
denotes |
This conclusion is in accord with data (Blumenthal, D. |
| T13 |
1673-1699 |
Sentence |
denotes |
K., Takio, K., Edelman, A. |
| T14 |
1700-1742 |
Sentence |
denotes |
M., Charbonneau, H., Titani, K., Walsh, K. |
| T15 |
1743-1760 |
Sentence |
denotes |
A., and Krebs, E. |
| T16 |
1761-1776 |
Sentence |
denotes |
G. (1985) Proc. |
| T17 |
1777-1782 |
Sentence |
denotes |
Natl. |
| T18 |
1783-1788 |
Sentence |
denotes |
Acad. |
| T19 |
1789-1793 |
Sentence |
denotes |
Sci. |
| T20 |
1794-1796 |
Sentence |
denotes |
U. |
| T21 |
1797-1799 |
Sentence |
denotes |
S. |
| T22 |
1800-1802 |
Sentence |
denotes |
A. |
| T23 |
1803-2182 |
Sentence |
denotes |
82, 3187-3191) that the carboxyl-terminal, 27-residue CNBr peptide of the native enzyme shows Ca2+-dependent, high affinity binding to calmodulin and that similar calmodulin-binding activity, although detectable in unfractionated CNBr digests of calmodulin-dependent enzyme forms, is much reduced in a CNBr digest of the calmodulin-independent, Mr = 35,000 chymotryptic fragment. |
| T1 |
0-110 |
Sentence |
denotes |
Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase. |
| T2 |
111-238 |
Sentence |
denotes |
Limited proteolysis has been utilized to study the structural organization of rabbit skeletal muscle myosin light chain kinase. |
| T3 |
239-555 |
Sentence |
denotes |
The enzyme (Mr approximately 89,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis) consists of an amino-terminal, protease-susceptible region of unidentified function and a carboxyl-terminal, protease-resistant region of Mr approximately 40,000 containing the catalytic and calmodulin-binding domains. |
| T4 |
556-737 |
Sentence |
denotes |
Partial digestion with trypsin produced an intermediate 56,000-dalton fragment and a stable 38,000-dalton fragment, both of which were catalytically active and calmodulin-dependent. |
| T5 |
738-850 |
Sentence |
denotes |
Chymotryptic digestion yielded three catalytically active fragments of about 37,000, 36,000, and 35,000 daltons. |
| T6 |
851-988 |
Sentence |
denotes |
The Mr = 37,000 fragment was calmodulin-dependent with an apparent affinity equivalent to that of the native enzyme (approximately 1 nM). |
| T7 |
989-1103 |
Sentence |
denotes |
The 36,000-dalton fragment was also calmodulin-dependent but had a approximately 200-fold lower apparent affinity. |
| T8 |
1104-1156 |
Sentence |
denotes |
The Mr = 35,000 fragment was calmodulin-independent. |
| T9 |
1157-1221 |
Sentence |
denotes |
These three chymotryptic fragments, had identical amino termini. |
| T10 |
1222-1440 |
Sentence |
denotes |
Nineteen residues were missing from the carboxyl terminus of the calmodulin-independent chymotryptic fragment whereas only 8 or 9 carboxyl-terminal residues were missing from the calmodulin-dependent tryptic fragments. |
| T11 |
1441-1617 |
Sentence |
denotes |
These results suggest that the 11-residue sequence (IAVSAANRFKK) in the carboxyl-terminal region of myosin light chain kinase contributes directly to the binding of calmodulin. |
| T12 |
1618-1672 |
Sentence |
denotes |
This conclusion is in accord with data (Blumenthal, D. |
| T13 |
1673-1699 |
Sentence |
denotes |
K., Takio, K., Edelman, A. |
| T14 |
1700-1742 |
Sentence |
denotes |
M., Charbonneau, H., Titani, K., Walsh, K. |
| T15 |
1743-1760 |
Sentence |
denotes |
A., and Krebs, E. |
| T16 |
1761-1776 |
Sentence |
denotes |
G. (1985) Proc. |
| T17 |
1777-1782 |
Sentence |
denotes |
Natl. |
| T18 |
1783-1788 |
Sentence |
denotes |
Acad. |
| T19 |
1789-1793 |
Sentence |
denotes |
Sci. |
| T20 |
1794-1796 |
Sentence |
denotes |
U. |
| T21 |
1797-1799 |
Sentence |
denotes |
S. |
| T22 |
1800-1802 |
Sentence |
denotes |
A. |
| T23 |
1803-2182 |
Sentence |
denotes |
82, 3187-3191) that the carboxyl-terminal, 27-residue CNBr peptide of the native enzyme shows Ca2+-dependent, high affinity binding to calmodulin and that similar calmodulin-binding activity, although detectable in unfractionated CNBr digests of calmodulin-dependent enzyme forms, is much reduced in a CNBr digest of the calmodulin-independent, Mr = 35,000 chymotryptic fragment. |