Tyrosination-detyrosination of tubulin and microtubules during the development of chick erythrocytes |
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Authors: | Dante M. Beltramo Carlos A. Arce Héctor S. Barra |
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Affiliation: | (1) Institute of Molecular Biology, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria |
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Abstract: | The protein composition of nuclear matrices containing different amount of DNA was examined. It was found that, in matrices containing 2% to 80% of total DNA, the quantity of DNA-bound proteins remains relatively constant varying from 10% to 15% of total nuclear proteins. Electrophoretic patterns do not differ substantially, but autoradiograms with in vitro125I labelled proteins show quantitative variations in the actin content. Application of radioimmunoassay (RIA) enabled to determine the exact content of actin in GAT nuclei and nuclear matrices – 5 g/ml in nuclei, of which 50% are bound to DNA and 3001o being a component of the protein part of the nuclear matrix. These results are supported by electron microscopic data, where immunogold technique was performed on thin sections and spread material. The applied methods suggest that part of the nuclear actin is tightly bound (resistant to 2 M NaCI) to DNA and represents a component of the internal nuclear matrix. |
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Keywords: | nuclear actin nuclear matrix immunoelectron microscopy |
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