Activity of chromatin-bound protease in histone fractions from rat liver and Morris hepatoma.
Activity of chromatin-bound protease of rat liver and Morris hepatoma 7777 was studied. Proteolytic enzyme was copurified with histones during extraction of chromatin with 0.25 M HCl. Total histone was fractionated by Oliver's et al. method. Histone fractions were incubated in 0.01 M Tris-HCl buffer (pH 7.6) at 37 degrees C within different periods of time. The behavior of these fractions in polyacrylamide gel electrophoresis as well as the amounts of peptides soluble in 5% TCA released during incubation indicated that enzyme was coextracted with histone H2B only. It was shown that the activity of protease coextracted selectively with histone H2B was higher in tumor tissue than in normal liver.
D000818:Animals; D002843:Chromatin / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008114:Liver Neoplasms, Experimental / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D051381:Rats
D002843:Chromatin; D006657:Histones; D010447:Peptide Hydrolases