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Deciphering a macro-troponin I complex; a case report

Clinical Chemistry and Laboratory Medicine (CCLM), 2017
Christopher M. Florkowski   +4 more
openaire   +3 more sources

Calcium binding by the troponin complex, and the purification and properties of troponin A

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
Abstract 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
openaire   +3 more sources

The Troponin Complex: Discriminating the Signal from the Noise

The American Journal of Medicine, 2022
Patients 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
openaire   +3 more sources

Lysine reactivities of tropomyosin complexed with troponin

Archives of Biochemistry and Biophysics, 1988
The 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
openaire   +3 more sources

Biology of the troponin complex in cardiac myocytes

Progress in Cardiovascular Diseases, 2004
Troponin 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
openaire   +3 more sources

Calcium-induced flexibility changes in the troponin C–troponin I complex

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
The 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
openaire   +3 more sources

Three-dimensional image reconstruction of actin-tropomyosin complex and actin-tropomyosin-troponin T-troponin I complex

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
openaire   +3 more sources

Design and Analytical Evaluation of Novel Cardiac Troponin Assays Targeting Multiple Forms of the Cardiac Troponin I-Cardiac Troponin T-Troponin C Complex and Fragmentation Forms.

Clinical Chemistry
BACKGROUND Current studies suggest that cardiac troponin (cTn) forms in the circulation may vary in different clinical scenarios. Our aim was to design a combination of cTn assays specific to the main cTn forms and to evaluate their analytical ...
Ling Li   +16 more
semanticscholar   +1 more source

The components of the troponin complex and development in skeletal muscle

Experimental Cell Research, 1980
Abstract 1. 1. Using the immunoperoxidase staining technique with monospecific antibodies to the polymorphic forms of the components of the troponin complex, two types of cells could be distinguished in rat leg muscles at 18 days' gestation. 2. 2.
S. Victor Perry, Gurtej K. Dhoot
openaire   +3 more sources

Proximity relationship in the binary complex formed between troponin I and troponin C

Journal of Molecular Biology, 1986
We have determined six molecular distances among four sites in the binary complex formed between troponin C (TnC) and troponin I (TnI) by fluorescence resonance energy transfer between donor and acceptor probes that were either an intrinsic fluorophore (Trp158 of TnI) or extrinsic probes attached to the sites.
Herbert C. Cheung, Chien-Kao Wang
openaire   +3 more sources

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