title: [Protease activity of the nuclear matrix of rat hepatocytes].
abstract: It was demonstrated that the nuclear matrix of rat liver possesses the protease activity. The specific activity of nuclear matrix proteases exceeds that of intact nuclei 7-fold. The optimum activity of nuclear matrix proteases is observed at pH 8-9. The protease activity of the nuclear matrix is inhibited by p-chloromercuribenzoate, N-ethylmaleimide, EDTA, phenylmethylsulfonyl fluoride. This suggests that thiol, serine and metalloproteases are associated with the nuclear matrix.
authors.forename: M P
authors.initials: MP
authors.lastname: Kutsyĭ
authors.forename: L V
authors.initials: LV
authors.lastname: Malakhova
authors.forename: A I
authors.initials: AI
authors.lastname: Gaziev
mesh_terms: D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors; D051381:Rats
chemical_list: D011480:Protease Inhibitors; D010447:Peptide Hydrolases
vernacular_title: Proteaznaia aktivnost' iadernogo matriksa gepatotsitov krys.