| Literature DB >> 1761526 |
M Ito1, Y Hirono, S Watanabe, H Yamamoto, K Maruyama.
Abstract
Immunofluorescence microscopy showed that a monoclonal antibody, 2F3, specific to the beta I subunit (Cap Z alpha) of beta-actinin (Cap Z) bound to the Z lines of chicken breast muscle. When myofibrils were briefly extracted with 0.6 M KI, the reactivity of the Z lines with 2F3 was very weak, but on subsequent treatment with purified beta-actinin, the antibody binding recovered. beta-Actinin inhibited elongation of the actin filaments of isolated I-Z-I brushes, myosin-extracted sarcomeres, on the addition of G-actin. However, when an increased concentration of G-actin was added, the inhibitory action of beta-actinin became negligible, suggesting that beta-actinin did not cap the pointed end of an actin filament in a myofibril.Entities:
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Year: 1991 PMID: 1761526 DOI: 10.1093/oxfordjournals.jbchem.a123575
Source DB: PubMed Journal: J Biochem ISSN: 0021-924X Impact factor: 3.387