title: Identification of troponin-I of crayfish myofibrils.
abstract: Crayfish (Procambarus clarkii) myofibrils contain two basic proteins of molecular weights of 25,000 and 23,000. Both of the two proteins inhibit actomyosin ATPase as the vertebrate troponin-I does. These results differ from the previous one that troponin-I of crayfish (Astacus leptodactylus) showed a single band on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE).
authors.affiliation: Department of Chemistry, Faculty of Science, Hokkaido University.
authors.forename: Y
authors.initials: Y
authors.lastname: Shinoda
authors.forename: A
authors.initials: A
authors.lastname: Yamada
authors.forename: K
authors.initials: K
authors.lastname: Yagi
mesh_terms: D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors; D000818:Animals; D003400:Astacoidea / Q000032:analysis*; D002118:Calcium / Q000502:physiology; D002147:Calmodulin / Q000502:physiology; D005591:Chemical Fractionation; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D009210:Myofibrils / Q000032:analysis*; D014336:Troponin / Q000032:analysis* / Q000502:physiology; D019210:Troponin I
chemical_list: D002147:Calmodulin; D014336:Troponin; D019210:Troponin I; D000251:Adenosine Triphosphatases; D002118:Calcium