Enhanced number of actin binding sites on plasma membranes of polyoma virus-transformed fibroblasts.
Plasma membranes, isolated from normal (C13) and polyoma virus-transformed (J1) cultured BHK cells were incubated with G-actin under polymerizing conditions, followed by a low-speed centrifugation. The amount of actin attached to the pelleted BHK-J1 plasma membranes was at least twice that on BHK-C13 membranes, indicating a greater number of actin attachment sites on the former. This result was confirmed by the observation that the plasma membranes from the transformed cells were also more active in nucleating polymerization of pyrene-labelled actin. Most of the actin attachment sites could be solubilized by Triton or low-salt extraction treatment.
Koffer
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Department of Biophysics, King's College, London, U.K.
Edgar
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D000199:Actins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002461:Cell Line, Transformed; D002462:Cell Membrane / Q000378:metabolism*; D002472:Cell Transformation, Viral; D005347:Fibroblasts; D017830:Octoxynol; D011092:Polyethylene Glycols / Q000494:pharmacology; D011120:Polyomavirus; D011817:Rabbits
D000199:Actins; D011092:Polyethylene Glycols; D017830:Octoxynol