Abstract：
: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.
journal_name
Neoplasmajournal_title
Neoplasmaauthors
Lipińska A,Krawczyk Z,Krajewska W,Kłyszejko-Stefanowicz L,Chorazy Msubject
Has Abstractpub_date
1980-01-01 00:00:00pages
409-13issue
4eissn
0028-2685issn
1338-4317journal_volume
27pub_type
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