Properties of chromosomal proteins of human leukemic cells.

Purified chromatin isolated from lymphocytic cells derived from patients with acute leukemia, or other lymphoproliferative disorders has been compared with chromatin isolated from normal human lymphocytic cells by gel electrophoresis and differential gradient ultracentrifugation. Thermal denaturation studies showed higher Tm values for chromatin from leukemic cells, as compared to that of lymphocytic cells from normal donors or patients with infectious mononucleosis, reflecting the diverse complexity of these chromatins with respect to their varying chemical compositions. There are significant differences in the ratios of DNA:RNA:protein, as well as in the ratios of chromatin-associated histone and non-histone proteins; although chromatin-associated histones were more homogeneous than were the non-histone proteins, as adjudged by amino acid analyses and acrylamide gel electrophoresis. These differences in chromatin structure may relate to the differences in gene expression characteristic of these lymphocytic cells. The chromosomal acidic proteins isolated from the purified chromatin of human leukemic cells greatly stimulated the template activity of the chromatin in in vitro RNA synthesis. The non-histone proteins selectively interact with chromatins and influence the RNA polymerase reactions, indicating that there is selective tissue specificity of non-histone proteins.