Abstract:
:The interaction of vinculin with actin filaments was investigated by methods which exclude interference by contaminating proteins which may occur in vinculin preparations. Vinculin which was blotted from SDS-polyacrylamide gels onto nitrocellulose, was stained specifically by fluorescently labeled polymeric actin (100 mM KCl, 2 mM MgCl2). Vinculin which was purified from alpha-actinin and an actin polymerization-inhibiting protein (HA1), was found to be cosedimented with polymeric actin. Maximally one vinculin molecule was cosedimented per one hundred actin filament subunits. Half maximal binding of vinculin was observed at about 0.25 microM free vinculin. Vinculin could be replaced from actin by the addition of tropomyosin.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ruhnau K,Wegner Adoi
10.1016/0014-5793(88)80595-7subject
Has Abstractpub_date
1988-02-08 00:00:00pages
105-8issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(88)80595-7journal_volume
228pub_type
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