scholarly journals Production, crystallization, and preliminary X-ray analysis of rabbit skeletal muscle troponin complex consisting of troponin C and fragment (1-47) of troponin I

1997 ◽  
Vol 6 (4) ◽  
pp. 916-918 ◽  
Author(s):  
Yumiko Saijo ◽  
Soichi Takeda ◽  
Anna Scherer ◽  
Tomoyoshi Kobayashi ◽  
Yuichiro Maéda ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Troponin C ◽  
Rabbit Skeletal Muscle ◽  
X Ray ◽  
Troponin Complex

scholarly journals Troponin C-like proteins (calmodulins) from mammalian smooth muscle and other tissues

1979 ◽  
Vol 177 (2) ◽  
pp. 521-529 ◽  
Author(s):  
R J Grand ◽  
S V Perry ◽  
R A Weeks
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Troponin I ◽  
Smooth Muscles ◽  
Bovine Brain ◽  
Troponin C ◽  
Rabbit Skeletal Muscle ◽  
Polyacrylamide Gels ◽  
Rabbit Lung ◽  
Chicken Gizzard

1. An acidic protein with properties similar to those of troponin C from rabbit skeletal muscle has been shown to be present in bovine and rabbit smooth muscles, chicken gizzard and rabbit liver, kidney and lung. 2. A simple new method involving the use of organic solvents is described for the purification of the troponin C-like proteins from various tissues. 3. The troponin C-like proteins can be distinguished from rabbit skeletal-muscle toponin C by their electrophoretic behaviour on polyacrylamide gels at pH 8.3 in the presence and absence of Ca2+. The troponin C-like proteins have been shown to form complexes with rabbit skeletal-muscle troponin I that migrate on electrophoresis in polyacrylamide gels. 4. Behaviour on electrophoresis, amino acid analysis and the patterns of CNBr digests on polyacrylamide gels indicate that the troponin C-like proteins from bovine uterus and aorta, rabbit uterus, and liver and chicken gizzard are very similar to, if not identical with, bovine brain modulator protein. 5. With bovine cardiac muscle the organic-solvent method yields a preparation consisting of roughly similar amounts of troponin C and troponin C-like protein. 6. By the isotope-dilution technique, troponin C-like protein has been shown to represent 0.42% of the total protein in rabbit uterus. 7. In homogenates of smooth muscle, rabbit lung, kidney and brain, the troponin C-like proteins form a complex with other protein (or proteins) that requires Ca2+ for its formation and that is not dissociated in 9M-urea.

Residues 48 and 82 at the N-Terminal Hydrophobic Pocket of Rabbit Skeletal Muscle Troponin-C Photo-Cross-Link to Met121 of Troponin-I†

Biochemistry ◽  
1999 ◽  
Vol 38 (20) ◽  
pp. 6678-6688 ◽  
Author(s):  
Yin Luo ◽  
John Leszyk ◽  
Yude Qian ◽  
John Gergely ◽  
Terence Tao
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Troponin C ◽  
Rabbit Skeletal Muscle ◽  
Cross Link ◽  
Hydrophobic Pocket

scholarly journals Calmodulin-free skeletal-muscle troponin C prepared in the absence of urea

1981 ◽  
Vol 195 (1) ◽  
pp. 205-211 ◽  
Author(s):  
J A Cox ◽  
M Comte ◽  
E A Stein
Keyword(s):  
Skeletal Muscle ◽  
Thiol Group ◽  
Troponin C ◽  
Rabbit Skeletal Muscle ◽  
Rapid Preparation ◽  
Step Procedure ◽  
Classical Procedure ◽  
Troponin Complex ◽  
One Step ◽  
Chromatography Step

A method is described for the rapid preparation of electrophoretically pure troponin C from rabbit skeletal-muscle myofibrils that avoids the use of urea. The three-step procedure includes extraction od the myofibrils with EDTA-containing buffers, one-step elution from DEAE-Sephadex and Sephadex G-100 chromatography in the presence of EDTA. The procedure gives yields comparable with those of currently used methods that involve dissociation of the troponin complex with urea. Except for the thiol-group reactivity, troponin C produced by our method is physicochemically and functionally indistinguishable from that obtained by the classical procedure. Purified troponin C always contains traces of calmodulin. However, this contamination can be decreased to less than 0.02% by means of a second Sephadex G-100 chromatography step in the presence of EDTA.

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