Polymorphism and tissue specificity of scallop tropomyosin

@article{Ishimodatakagi1986PolymorphismAT,
  title={Polymorphism and tissue specificity of scallop tropomyosin},
  author={T. Ishimoda-takagi and Mitsuaki Kobayashi and Masako Yaguchi},
  journal={Comparative Biochemistry and Physiology B},
  year={1986},
  volume={83},
  pages={515-521}
}

Heterogeneity and tissue specificity of tropomyosin isoforms from four species of bivalves.

Fish fast skeletal muscle tropomyosins show species-specific thermal stability.

Tissue specificity of tropomyosin isoform in the mussel, Mytilus galloprovincialis

In the mussel, Mytilus galloprovincialis, there were three kinds of tropomyosin isoforms, which were designated as TM1, TM2 and TM3, respectively, but TM2and TM3 were detected as two new isoforms in the mantle and gills.

Thermostability of striated and smooth adductor muscle tropomyosins from Yesso scallop Mizuhopecten yessoensis.

Results suggest that smooth muscle TM has higher thermostability than striated muscle TM and the amino acid residues responsible for such stability difference were considered to be the six amino acid substitutions in the middle region of the TM molecules.

Tropomyosin Is the Major Mollusk Allergen: Reverse Transcriptase Polymerase Chain Reaction, Expression and IgE Reactivity

Results demonstrate that tropomyosin is the major allergen among various common edible mollusks and a comparison between the amino acid sequences of putative epitopes in crustaceans and mollUSks suggests that the epitope in the two groups may be distinct.

Invertebrate muscles: muscle specific genes and proteins.

This is the first of a projected series of canonic reviews covering all invertebrate muscle literature prior to 2005 and covers muscle genes and proteins except those involved in excitation-contraction coupling and those forming ligand- and voltage-dependent channels.

Effect of trichloroacetic acid on the isolation of tropomyosin from sea urchin lantern muscle.

Sea urchin lantern muscle tropomyosin showed two components in sodium dodecyl sulfate (SDS) gel electrophoresis in the presence of 5 M urea, although the molecular weights of these components were

Chemical and immunochemical characteristics of tropomyosins from striated and smooth muscle.

1. On electrophoresis in dissociating conditions the tropomyosins isolated from skeletal muscles of mammalian, avian and amphibian species migrated as two components. These were comparable with the

Immunological purification of sea urchin egg tropomyosin.

The presence of tropomyosin in the sea urchin egg was shown by immunodiffusion test between the antiserum and the egg tropomeosin fraction which was prepared according to the purification method for muscle tropomyOSin.

The subunits and biological activity of polymorphic forms of tropomyosin.

The activity of tropomyosin on the Mg(2+)-stimulated ATPase in the regulatory-protein system was more susceptible to enzymic digestion and thermal denaturation than its effect on the Ca(2)+)-stimulating ATPase of actomyOSin.

The species specifity of the contractile protein composition of the bivalve molluscs.

  • B. MargulisG. Pinaev
  • Environmental Science, Biology
    Comparative biochemistry and physiology. B, Comparative biochemistry
  • 1976

On the heterogeneity and organ specificity of chicken tropomyosins.

Tropomyosins from chicken cardiac, skeletal, and gizzard muscles were each resolved into two subunits by polyacrylamide gel electrophoresis in a system containing sodium dodecylsulfate, urea and sodium borate and Immunological evidence presented indicates that each subunit has a specific antigenic site in addition to an identical one(s) in common with the others.

Tropomyosin isoforms in chicken embryo fibroblasts: purification, characterization, and changes in Rous sarcoma virus-transformed cells

It is found that major tropomyosin 1 was greatly reduced in transformed cells and the relative amounts of tropomyOSin 3a and 3b were increased in both the total cell lysate and the microfilament fraction of transformed cells, which may reflect the in vivo assembly of tropomeosin isoforms.