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Proteins of the Troponin Complex [PDF]
Laboratory Medicine, 1992 The troponin complex is a group of three protein subunits located on the thin filament of the contractile apparatus. These three subunits—troponin T, troponin I, and troponin C—different in genetic and protein structure, act together to regulate muscle contraction.
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RESOLUTION OF BRAIN TROPONIN COMPLEX
Journal of Neurochemistry, 1979AbstractAffinity chromatography was used to partially purify the troponin complex from crude regulatory proteins obtained from bovine brain cortex. Three components were obtained from this partially purified troponin complex by treatment with 6 M‐urea and 1 mM‐EGTA followed by chromatography on DEAE‐Sephadex‐A50.
C. Mahendran, S. Berl
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Calcium binding by the troponin complex, and the purification and properties of troponin A
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971Abstract The percentage of tropomyosin and troponin in rabbit psoas muscle was estimated to be 4.2% and 5.6% of the myofibrillar protein, respectively. This suggests that on the thin filament there are two molecules of tropomyosin per 390 A, and probably two molecules of the troponin complex.
H.Y. Pyun, D.J. Hartshorne
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The Troponin Complex: Discriminating the Signal from the Noise
The American Journal of Medicine, 2022Patients presenting to the emergency department with consideration of an acute coronary syndrome (ACS) are risk-stratified with sensitive troponin assays. Among many patients who present with symptoms other than chest pain, they are admitted for observation if the troponin assay is above the upper reference limit of that specific assay. With the advent
Ion S. Jovin, Edward O. McFalls
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The troponin complex and regulation of muscle contraction
The FASEB Journal, 1995In a wide variety of cellular settings, from organelle transport to muscle contraction, Ca2+ binding to members of the EF hand family of proteins controls the interaction between actin and different myosins that are responsible for generating movement. In vertebrate skeletal and cardiac muscle the Ca(2+)-binding protein troponin C (TnC) is one subunit ...
Fernando C. Reinach, Chuck S. Farah
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Lysine reactivities of tropomyosin complexed with troponin
Archives of Biochemistry and Biophysics, 1988The relative reactivities of lysine residues of tropomyosin complexed with troponin have been measured in order to locate the binding site of troponin on tropomyosin in a complex between the two native proteins. The lysines were labeled with acetic anhydride using a competitive labeling procedure and the relative reactivities of tropomyosin lysine ...
Sarah E. Hitchcock-DeGregori +5 more
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Biology of the troponin complex in cardiac myocytes
Progress in Cardiovascular Diseases, 2004Troponin is the regulatory complex of the myofibrillar thin filament that plays a critical role in regulating excitation-contraction coupling in the heart. Troponin is composed of three distinct gene products: troponin C (cTnC), the 18-kD Ca(2+)-binding subunit; troponin I (cTnI), the approximately 23-kD inhibitory subunit that prevents contraction in ...
R. John Solaro, Michael S. Parmacek
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Physarum Tropomyosin-Troponin Complex
The Journal of Biochemistry, 1975The relaxing protein (TM-TN complex) was isolated from plasmodia of Physarum. SDS-gel electrophoresis revealed that the relaxing protein consists of tropomyosin subunits with a molecular weight of 35,000 troponin subunits with molecular weights of 38,000 (T) and 24,000 (I) and several other components. No component corresponding to muscle troponinC (MW-
Yuji Tonomura, Toyoki Kato
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Calcium-induced flexibility changes in the troponin C–troponin I complex
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000The contraction of vertebrate striated muscle is modulated by Ca(2+) binding to the regulatory protein troponin C (TnC). Ca(2+) binding causes conformational changes in TnC which alter its interaction with the inhibitory protein troponin I (TnI), initiating the regulatory process.
John H. Collins +9 more
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Journal of Molecular Biology, 1975
Abstract The structure of the actin-tropomyosin complex, which represents on active form of the thin filaments of skeletal muscle and the actin-tropomyosin-troponin T-troponin I complex, which represents an inhibited form, have been studied by three-dimensional reconstruction from electron micrographs.
Hugh E. Huxley +3 more
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Abstract The structure of the actin-tropomyosin complex, which represents on active form of the thin filaments of skeletal muscle and the actin-tropomyosin-troponin T-troponin I complex, which represents an inhibited form, have been studied by three-dimensional reconstruction from electron micrographs.
Hugh E. Huxley +3 more
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