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Identification of actin from hepatoma Morris 5123 cells

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Nowak D., Kochman A., Malicka-Błaszkiewicz M.
Acta Biochimica Polonica
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1999
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vol. 46
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issue 4
949-959
EN
The hepatoma Morris 5123 tumor growth is accompanied by changes in actin content and polymerization (Malicka-Błaszkiewicz et al. (1995) Mat. Med. Pol., 27, 115-118;  Nowak et al. (1995) J. Exp. Cancer Res. 14, 37-40). Presently actin isoforms from cytosol and  cytoskeleton fractions were separated by SDS/PAGE and identified with antibodies directed against different actin isoforms. Actin isolated from the cytosol by affinity chromatography on DNase I bound to agarose shows the presence of only one protein spot on 2D gel electrophoresis corresponding to the mobility of the rabbit α skeletal muscle actin (M^r 43000) and isoelectric point equal to 5.3. It interacts only with monoclonal anti β actin isoform antibodies, posing the question of differential affinity of actin isoforms to DNase I.
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