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. 1999 Aug 23;146(4):831–842. doi: 10.1083/jcb.146.4.831

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© 1999 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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CH1 domain of fimbrin binds the NH₂ terminus of nonassembled vimentin. (A) In vitro expressed and purified wild type (WT), COOH-terminally deleted (N410) or NH₂-terminally deleted (102C) vimentin were resolved on SDS-PAGE, transferred to PVDF, and probed with labeled fimbrin. Fimbrin binds wild type (WT) and the COOH-terminally deleted vimentin (N410) but not the NH₂-terminal deleted vimentin (102C). (B) Limited proteolysis of fimbrin with Lys-C and the fragments were detected with silver stain (lane 1), electroblotted, and probed with biotinylated vimentin (lane 2). Vimentin bound a 26-kD fragment. (C) Overlays of fimbrin deletion constructs using biotinylated vimentin. Vimentin bound bands that contained residues 143–188 in the CH1 domain.