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. 2001 May 28;153(5):1035–1048. doi: 10.1083/jcb.153.5.1035

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© 2001 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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(A) SDS-PAGE of purified fish actin (right lane) after Coomasie blue staining. The presence of only one major band at the 43-kD marker position (left lane) confirms the purity of extracted actin. (B) Spectrofluorophotometric data from in vitro acrylodan actin polymerization assay under different conditions as indicated, demonstrating the loss of actin-sequestering capability of Tβ4 as a result of caging with NVOC (molar ratio of caged Tβ4/actin was equal to 4:1). Uncaging restored the biochemical activity of caged Tβ4, comparable to the efficiency of pure Tβ4. (C) Western blot of keratocyte scale extracts with anti-Tβ4 antibody (right lane). GST-Tβ4 served as a positive control for the antibody binding (left lane). (D) Immunostaining of Tβ4 in keratocytes demonstrating its diffuse intracellular distribution.