Tropomyosin is in a reduced state in rabbit psoas muscle
نویسندگان
چکیده
منابع مشابه
Fragments of Rabbit Striated Muscle a - Tropomyosin
The interactions of a variety of large fragments of rabbit skeletal muscle a-tropomyosin, prepared as previously described, with troponin-T and a soluble tropomyosin-binding fragment of troponin-T (CB1) have been investigated by affinity chromatography and gel filtration. No specific interactions between NHz-terminal fragments encompassing residues 1-189 with troponin, troponin-T, or CB1 immobi...
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The binding of 125I-labeled muscle tropomyosin to Acanthamoeba and muscle actin was studied by ultracentrifugation and by the effect of tropomyosin on the actin-activated muscle heavy meromyosin ATPase activity. Binding of muscle tropomyosin to Acanthamoeba actin was much weaker than its binding to muscle actin. For example, at 5 mM MgCl2, 2 mM ATP, and 5 micronM actin, tropomyosin bound strong...
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since the 1960s the age effects on learning both first and second language have been explored by many linguists and applied linguists (e.g lennerberg, 1967; schachter, 1996; long, 1990) and the existence of critical period for language acquisition was found to be a common ground of all these studies. in spite of some common findings, some issues about the impacts of age on acquiring a second or...
15 صفحه اولRigor cross-bridges bind to two actin monomers in thin filaments of rabbit psoas muscle.
The mode of binding of myosin subfragment-1 (S1) to actin is known to depend on their molar ratio: when actin is in excess, S1 binds to two actin monomers within the actin filament, and when S1 is in excess or is equimolar with actin, each S1 binds to one actin monomer. Since in vertebrate striated muscle actin is in molar excess over myosin, we expect that in fibers each myosin head binds to t...
متن کاملThe relaxed crossbridge pattern in isolated rabbit psoas muscle thick filaments.
Rabbit muscle is a major source of material for biochemical experiments and spin labelling studies of contraction, and so it is important to establish how closely this material resembles the frog and fish muscles usually used for structural studies. Previous studies have shown that relaxed rabbit muscle thick filaments lose the characteristic order of their crossbridges when they are cooled bel...
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ژورنال
عنوان ژورنال: Journal of Muscle Research and Cell Motility
سال: 2011
ISSN: 0142-4319,1573-2657
DOI: 10.1007/s10974-011-9249-6