title: Beta-actinin is not distinguishable from an actin barbed-end capping protein in chicken breast muscle.
abstract: beta-Actinin is an actin-pointed end capping protein in skeletal muscle. Casella et al. have reported that a protein isolated from muscle acetone powder by procedures similar to those used for beta-actinin purification caps the barbed end of an actin filament (J. Biol. Chem. 261, 10915-10921 (1986)). We have confirmed the above results. However, it turned out that the two proteins were identical as to subunit sizes, peptide maps, and cross-reactivities with anti-beta-actinin IgG. The binding of the two proteins to opposite ends of an actin filament remains unexplained.
authors.affiliation: Department of Biology, Faculty of Science, Chiba University.
authors.forename: M
authors.initials: M
authors.lastname: Oosawa
authors.forename: S
authors.initials: S
authors.lastname: Shimaoka
authors.forename: T
authors.initials: T
authors.lastname: Funatsu
authors.forename: S
authors.initials: S
authors.lastname: Ishiwata
authors.forename: K
authors.initials: K
authors.lastname: Maruyama
mesh_terms: D051339:Actin Depolymerizing Factors; D000199:Actins / Q000302:isolation & purification; D000818:Animals; D002645:Chickens; D051345:Destrin; D004591:Electrophoresis, Polyacrylamide Gel; D007158:Immunologic Techniques; D007525:Isoelectric Focusing; D008840:Microfilament Proteins / Q000302:isolation & purification; D009132:Muscles / Q000032:analysis*
chemical_list: D051339:Actin Depolymerizing Factors; D000199:Actins; D051345:Destrin; D008840:Microfilament Proteins