[Action of dithiothreitol on protein pattern and phosphorylation in nuclear matrix preparations isolated from the rat liver and Zajdela's hepatoma].

After rat liver nuclei had been treated with 10 mM dithiothreitol nuclear matrix contained 40 per cent less protein than without treatment. Protein composition did not change qualitatively. The protein with a molecular weight of 35 kD was not phosphorylated in the treated samples. After Zajdela hepatoma nuclei had been treated in the same way, nuclear-matrix contained 25% less protein. High molecular weight proteins (140, 150 and 220 kD) were solubilized by media containing dithiothreitol. After dithiothreitol treatment phosphatase and protein-phosphatase activities reduced dramatically both in rat liver and Zajdela hepatoma nuclear matrices.