Alteration of glycoproteins in nuclei during regeneration of rat liver.

Hepatocyte nuclei from partially hepatectomized and sham operated rats were isolated. Total and 0.35 M NaCl soluble proteins were prepared from the nuclei. The proteins were separated by gel electrophoresis and examined by lectin staining methods. Within the limits of sensitivity of these techniques, the following features emerged. 1) A majority of proteins visualized were common to and present in similar relative quantities in the nuclei during rat liver regeneration. 2) The nuclear glycoproteins were detected by several lectins. The fluctuations at the stages of the regeneration were evident. The complicated patterns of changes were observed. 3) The DNA binding activities of the nuclear proteins were observed by the south-western methods. The DNA binding activities of nuclear proteins were changed after enzyme digestion of sugar moieties of nuclear glycoproteins. From these of our results, it is suggested that the sugar chains of nuclear glycoproteins play important roles of DNA binding activities of the nuclear proteins.