Results 351 to 360 of about 6,673,815 (394)

Ca2+ dependence of the distance between Cys-98 of troponin C and Cys-133 of troponin I in the ternary troponin complex. Resonance energy transfer measurements.

Biochemistry, 1989
We have used resonance energy transfer to study the spatial relationship between Cys-98 of rabbit skeletal troponin C and Cys-133 of rabbit skeletal troponin I in the reconstituted ternary troponin complex.
T. Tao, E. Gowell, G. Strasburg, J. Gergely, P. Leavis   +4 more
semanticscholar   +1 more source

The highly conserved COOH terminus of troponin I forms a Ca2+-modulated allosteric domain in the troponin complex.

Biochemistry, 2001
The primary structure of the COOH-terminal region of troponin I (TnI) is highly conserved among the cardiac, slow, and fast skeletal muscle TnI isoforms and across species.
Jian Ping Jin, Fang-Wei Yang, Zhi-Bin Yu, Cristian I. Ruse, Meredith Bond, Aihua Chen   +5 more
semanticscholar   +1 more source

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
openaire   +3 more sources

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
openaire   +3 more sources

Assembly of functional skeletal muscle troponin complex in Escherichia coli.

European Journal of Biochemistry, 1994
The production of multi-subunit proteins of eukaryotic origin in Escherichia coli usually relies on the different subunits being expressed individually and the protein being reassembled in vitro.
Bettina Malnic, F. Reinach
semanticscholar   +1 more source

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
openaire   +3 more sources

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
openaire   +3 more sources

Troponin T and Ca2+ dependence of the distance between Cys48 and Cys133 of troponin I in the ternary troponin complex and reconstituted thin filaments.

Biochemistry, 1997
Contraction of vertebrate striated muscle is regulated by the interaction of Ca2+ with the heterotrimeric protein troponin (Tn), composed of troponin-C (TnC), troponin-I (TnI), and troponin-T (TnT).
Y. Luo, J. Wu, J. Gergely, T. Tao
semanticscholar   +1 more source

The Crystal Structure of Troponin C in Complex with N-Terminal Fragment of Troponin I

1998
Troponin (Tn), the complex of three subunits (TnC, TnI, and TnT), plays a key role in Ca2+ dependent regulation of muscle contraction. To elucidate the interactions between the Tn subunits and the conformation of TnC in the Tn complex, we have determined the crystal structure of TnC in complex with the N-terminal fragment of TnI (TnI1-7). The structure
Soichi Wakatsuki, Kayo Maeda, Soichi Takeda, Yuichiro Maéda, Dmitry G. Vassylyev   +4 more
openaire   +2 more sources

MOLECULAR PROPERTIES OF POSTMORTEM MUSCLE. 8. Effect of Postmortem Storage on α‐Actinin and the Tropomyosin‐Troponin Complex

, 1970
SUMMARY– Effects of postmortem storage of rabbit muscle at 25° on the properties of α-actinin and tropomyosin-troponin-containing fractions prepared from this muscle were studied.
N. Arakawa, D. E. Goll, J. Temple
semanticscholar   +1 more source