Results 271 to 280 of about 43,375 (307)

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
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Structure of the insect troponin complex 1 1Edited by M. F. Moody

Journal of Molecular Biology, 1999
Isolated troponin-tropomyosin complex from Lethocerus indicus asynchronous flight muscle forms paracrystals on a positively charged lipid monolayer. Single particle analysis was carried out on individual complexes selected from electron micrographs of negatively stained paracrystals.
Thomas Wendt, Kevin Leonard
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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
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Human cardiac troponin complex. Structure and functions

Biochemistry (Moscow), 2013
Troponin complex is a component of skeletal and cardiac muscle thin filaments. It consists of three subunits - troponin I, T, and C, and it plays a crucial role in muscle activity, connecting changes in intracellular Ca2+ concentration with generation of contraction.
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Binding of Troponin I and the Troponin I−Troponin C Complex to Actin−Tropomyosin. Dissociation by Myosin Subfragment 1

Biochemistry, 2000
Troponin I (TnI) is the component of the troponin complex, TnI, TnC, TnT, that is responsible for inhibition of actomyosin ATPase activity. Using the fluorescence of pyrene-labeled tropomyosin (Tm), we probed the interaction of TnI and TnIC with Tm on the reconstituted muscle thin filament.
X Zhou, E P Morris, Sherwin S. Lehrer
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A Binary Complex of Troponin-I and Troponin-T from Akazara Scallop Striated Adductor Muscle1

The Journal of Biochemistry, 1991
A binary complex consisting of Mr 19,000 and Mr 40,000 components was co-purified with troponin from a crude troponin fraction of Akazara scallop (Chlamys nipponensis akazara) striated adductor muscle. This complex is incapable of conferring Ca(2+)-sensitivity to rabbit reconstituted actomyosin Mg-ATPase activity, rather strongly inhibiting it, but ...
Takao Ojima, Kiyoyoshi Nishita
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An immunochemical study of the calcium ion-binding protein (troponin-C) and the inhibitory protein (troponin-I) of the troponin complex and their interaction

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1974
1. 1.|Antibodies to troponin-C and troponin-I, prepared by a preparative acrylamide gel electrophoresis, have been studied by Ouchterlony's immunodiffusion procedure. 2. 2.|In amino acid composition and antigenic properties, troponin-C of chicken skeletal muscle resembled the troponin-C from skeletal muscle of other animals more closely than ...
S.V. Perry, T. Hirabayashi
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Extraction and Replacement of the Tropomyosin–Troponin Complex in Isolated Myofibrils

2010
Tropomyosin (Tm) is an essential component in the regulation of striated muscle contraction. Questions about Tm functional role have been difficult to study because sarcomere Tm content is not as easily manipulated as Troponin (Tn). Here we describe the method we recently developed to replace Tm-Tn of skeletal and cardiac myofibrils from animals and ...
SCELLINI, BEATRICE, PIRODDI, NICOLETTA, POGGESI, CORRADO, TESI, CHIARA   +3 more
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Cross-linking of rabbit skeletal muscle troponin subunits: labeling of cysteine-98 of troponin C with 4-maleimidobenzophenone and analysis of products formed in the binary complex with troponin T and the ternary complex with troponins I and T

Biochemistry, 1988
The sulfhydryl-specific, heterobifunctional, photoactivatable cross-linker 4-maleimidobenzophenone (BPMal) was used to study the interaction of rabbit skeletal muscle troponin subunits TnC, TnT, and TnI. TnC was labeled at Cys-98 by the maleimide moiety of BPMal and then mixed with either TnT alone or TnI plus TnT, in the presence of Ca2+.
Terence Tao, John D. Leszyk, Paul C. Leavis, John H. Collins   +3 more
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Proximity Relationships between Residue 6 of Troponin I and Residues in Troponin C:  Further Evidence for Extended Conformation of Troponin C in the Troponin Complex

Biochemistry, 2000
Skeletal muscle troponin C (TnC) adopts an extended conformation when crystallized alone and a compact one when crystallized with an N-terminal troponin I (TnI) peptide, TnI(1-47) [Vassylyev et al. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 4847-4852]. The N-terminal region of TnI (residues 1-40) was suggested to play a functional role of facilitating ...
John D. Leszyk, John Gergely, Bing Li, Yin Luo, Terence Tao   +4 more
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