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Tropomyosin antibody: the specific localization of tropomyosin in nonmuscle cells. [PDF]
Journal of Cell Biology, 1975 An antibody against purified chicken skeletal muscle tropomyosin is used in indirect immunofluorescence to visualize the localization of tropomyosin in a variety of nonmuscle cells. The antibody produces a fluorescent pattern which is very similar to that obtained with an actin-specific antibody. This pattern is composed of fluorescent fibers which are
E Lazarides, Lazarides E
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On the polymerization of tropomyosin
Archives of Biochemistry and Biophysics, 1962Abstract The polymerization of tropomyosin was studied by light scattering, covering a wide range of protein and salt concentrations. Depolymerization of tropomyosin molecules with dilution was found at very dilute protein concentration, a phenomenon which had not been observed.
T, OOI, K, MIHASHI, H, KOBAYASHI
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β‐Tropomyosin mutations alter tropomyosin isoform composition
European Journal of Neurology, 2008Background and purpose: Tropomyosin (TM) is an actin‐binding protein, which is localized head to tail along the length of the actin filament. There are three major TM isoforms in human striated muscle. Mutations in β‐tropomyosin (TPM2) have recently been identified as an important cause of neuromuscular disorders.
J, Nilsson, H, Tajsharghi
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Proceedings of the Royal Society of London. Series B - Biological Sciences, 1953
Abstract In all muscles so far examined there is present an unusual protein to which no function has yet been assigned. It occurs side by side with actin and myosin in the myofibril, and because of its similarity to myosin was named tropomyosin (Bailey 1948).
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Abstract In all muscles so far examined there is present an unusual protein to which no function has yet been assigned. It occurs side by side with actin and myosin in the myofibril, and because of its similarity to myosin was named tropomyosin (Bailey 1948).
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Journal of Muscle Research and Cell Motility, 2014
Tropomyosin is a two chained α-helical coiled coil protein that binds actin filaments and interacts with various actin binding proteins. Tropomyosin function depends on its ability to move to distinct locations on the surface of actin in response to the binding of different thin filament effectors.
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Tropomyosin is a two chained α-helical coiled coil protein that binds actin filaments and interacts with various actin binding proteins. Tropomyosin function depends on its ability to move to distinct locations on the surface of actin in response to the binding of different thin filament effectors.
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Tryptic Digestion of Tropomyosin A, Tropomyosin B and Myosin
Nature, 1966Two types of tropomyosins co-exist in lamellibranch adductors and in cephalopod muscle1: TMA and TMB, TMA being the protein referred to as invertebrate tropomyosin, or water-insoluble tropomyosin, by Bailey, and TMB the water-soluble variety.
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Cold Adaptation of Tropomyosin
Biochemistry, 2011The conformational stability of unphosphorylated and phosphorylated α,α-striated tropomyosins from rabbit and shark (95% identical sequences) has been investigated. Three additional core positions are occupied by atypical amino acids in the protein from shark: Thr179(d), Ser190(a), and Ser211(a).
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Vertebrate and Invertebrate Tropomyosins
Nature, 1957AS a first step toward generalizing the relationship between tropomyosin, actin and myosin found for rabbit skeletal muscle1, we have prepared and examined tropomyosins from the different types of mammalian muscle (cardiac, uterine and smooth), from lower classes within the vertebrate phylum (amphibian, fish and cyclostome) and from representatives of ...
D R, KOMINZ, K, LAKI, F, SAAD
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