Association of three chicken proteins with the 34 kD target of rous sarcoma virus tyrosine kinase |
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Authors: | M. Simon A. -P. Arrigo P. -F. Spahr |
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Affiliation: | 1. University of Massachusetts, Department of Orthopaedic Surgery, Worcester, MA, United States;2. University of Kentucky School of Medicine, Department of Orthopaedic Surgery and Sports Medicine, Lexington, KY, United States |
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Abstract: | Transformation of chicken embryo fibroblasts by avian retroviruses induces the tyrosine phosphorylation of a 34-39 kD cellular protein (p34). In vitro, p34 isolated from intestine interacts with F-actin in a Ca2+-dependent manner. We report here that, in the absence of Ca2+ chelators, three proteins co-purified with p34 extracted from a cytosolic or membrane fraction of chicken embryo fibroblasts; these two fractions account respectively for 10-20% and 50% of the total cellular p34. Isolated from the cytosoluble fraction of fibroblasts by sucrose gradient centrifugation and hydrophobic chromatography, p34 and the other proteins behaved as a homogeneous species upon non-denaturing gel electrophoresis, gel filtration, and CsCl density gradient centrifugation, thus indicating a strong association. Moreover, an analysis by electron microscopy following uranyl acetate staining revealed particles with a raspberry-like shape. This association was always disrupted by the calcium-chelating agent, EGTA. |
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