Distribution of antibodies to the troponin complex, troponin-C and troponin-I in chicken skeletal muscle as determined by a simplified method for immuno-electron microscopy

1977 ◽  
Vol 9 (2) ◽  
pp. 273-284 ◽  
Author(s):  
Frank J. Wilson ◽  
Tamio Hirabayashi ◽  
Mei Cheng
Keyword(s):  
Electron Microscopy ◽  
Skeletal Muscle ◽  
Troponin I ◽  
Troponin C ◽  
Simplified Method ◽  
Immuno Electron Microscopy ◽  
Troponin Complex ◽  
Chicken Skeletal Muscle

Ca2+, Mg2+, and Troponin I Inhibitory Peptide Binding to a Phe-154 to Trp Mutant of Chicken Skeletal Muscle Troponin C

Biochemistry ◽  
1994 ◽  
Vol 33 (10) ◽  
pp. 2961-2969 ◽  
Author(s):  
Murali Chandra ◽  
William D. McCubbin ◽  
Kim Oikawa ◽  
Cyril M. Kay ◽  
Lawrence B. Smillie
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Peptide Binding ◽  
Troponin C ◽  
Inhibitory Peptide ◽  
Trp Mutant ◽  
Chicken Skeletal Muscle

scholarly journals Immunohistochemical and ultrastructural distribution of antibodies to troponin-C and troponin-I in normal and dystrophic chicken skeletal muscle.

1978 ◽  
Vol 26 (4) ◽  
pp. 258-266 ◽  
Author(s):  
F J Wilson ◽  
D Camiscoli ◽  
M J Irish ◽  
T Hirabayashi
Keyword(s):  
Troponin I ◽  
Pectoral Muscle ◽  
Troponin C ◽  
Dystrophic Muscle ◽  
Ultrastructural Studies ◽  
Antigenic Sites ◽  
Immuno Electron Microscopy ◽  
And Control ◽  
Chicken Skeletal Muscle ◽  
Dystrophic Chicken

The pectoral muscles from normal and dystrophic chickens were reacted with rabbit antisera to troponin-C and to troponin-I, and the distribution of antibodies was determined by fluorescence microscopy of antibody-stained myofibrils and immuno-electron microscopy of separated I band segments. Chickens of dystrophic strain 308 and control New Hampshire hens were used in this work. Myofibrils which were prepared from both normal and dystrophic muscles and reacted with anti-troponin-I were fluorescent in the I band and A band regions. The Z lines and H zones were unstained. Myofibrils prepared from normal pectoral muscle and treated with anti-troponin-C yielded a pattern of fluorescence similar to that for anti-troponin-I treated myofibrils. However, those myofibrils isolated from dystrophic muscle and reacted with anti-tropinin-C had a weak fluorescence over their entire lengths, and discrete A- and I-band staining was not visible. These results were confirmed by ultrastructural studies of separated I segments reacted with the antisera. It is concluded that in the dystrophic muscle either the antigenic sites of troponin-C are changed which results in a loss of antibody-combining ability or these sites are masked in some way which prevents the reaction with the antibody.

scholarly journals Studies of the interaction of troponin I with proteins of the I-filament and calmodulin

1983 ◽  
Vol 209 (2) ◽  
pp. 417-426 ◽  
Author(s):  
A J G Moir ◽  
M Ordidge ◽  
R J A Grand ◽  
I P Trayer ◽  
S V Perry
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Troponin C ◽  
Sedimentation Equilibrium ◽  
Equilibrium Studies ◽  
Troponin Complex ◽  
Lysine Residues ◽  
C Complex ◽  
Modes Of Interaction ◽  
Fast Twitch

1. All lysine residues in native troponin I from rabbit fast-twitch skeletal muscle reacted with methyl acetimidate and ethyl acetimidate. 2. The reactivity of lysine-18 of troponin I to acetimidate was much diminished when the troponin I was complexed in the presence of Ca2+ with troponin C alone or in the whole troponin complex. 3. In the presence of EGTA, lysine-18 of troponin I in the troponin I-troponin C complex was more reactive to acetimidate than it was in the presence of Ca2+. 4. No masking of lysine residues could be detected when troponin I interacted with calmodulin or actin. 5. Sedimentation-equilibrium studies indicated that the complex of troponin I with calmodulin was more readily dissociated in the absence of Ca2+ than was its complex with troponin C under otherwise identical conditions. 6. These studies suggest that the nature of the involvement of the N-terminal region of troponin I is a major difference between its modes of interaction with calmodulin and with troponin C.

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 Cloning and expression of chicken skeletal muscle troponin I inEscherichia coli: The role of rare codons on the expression level

1993 ◽  
Vol 2 (6) ◽  
pp. 1053-1056 ◽  
Author(s):  
Ronaldo B. Quaggio ◽  
Jesus A. Ferro ◽  
Patricia B. Monteiro ◽  
Fernando C. Reinach
Keyword(s):  
Skeletal Muscle ◽  
Troponin I ◽  
Cloning And Expression ◽  
Expression Level ◽  
Inescherichia Coli ◽  
Rare Codons ◽  
Chicken Skeletal Muscle

Structure of chicken skeletal muscle troponin C at 1.78 Å resolution

1994 ◽  
Vol 50 (1) ◽  
pp. 40-49 ◽  
Author(s):  
K. A. Satyshur ◽  
D. Pyzalska ◽  
M. Greaser ◽  
S. T. Rao ◽  
M. Sundaralingam
Keyword(s):  
Skeletal Muscle ◽  
Troponin C ◽  
Chicken Skeletal Muscle
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