title: [Domain organization of alpha-actinin from the rabbit skeletal muscle].
abstract: Limited trypsinolysis of native alpha-actinin by trypsin was carried out. This procedure resulted in the formation of two large fragments with Mr of 30 and 70 kD which cover almost the whole subunit of alpha-actinin. Using the sedimentation equilibrium method, it was demonstrated that the bisubunit structure of alpha-actinin is provided for by C-terminal fragments of the subunits. Data from circular dichroism analysis suggest that the fragments formed are independent structural units, i.e., domains.
authors.forename: K Sh
authors.initials: KSh
authors.lastname: Kuridze
authors.forename: S Iu
authors.initials: SIu
authors.lastname: Ven'iaminov
authors.forename: M Sh
authors.initials: MSh
authors.lastname: Simonidze
authors.forename: N Sh
authors.initials: NSh
authors.lastname: Nadirashvili
authors.forename: M M
authors.initials: MM
authors.lastname: Zaalishvili
mesh_terms: D000185:Actinin / Q000032:analysis* / Q000648:ultrastructure; D000818:Animals; D002942:Circular Dichroism; D006868:Hydrolysis; D008854:Microscopy, Electron; D008970:Molecular Weight; D009132:Muscles / Q000032:analysis*; D011487:Protein Conformation; D011817:Rabbits
chemical_list: D000185:Actinin
vernacular_title: Domennaia organizatsiia alpha-aktinina skeletnoĭ myshtsy krolika.