title: Potentiation of cysteine proteinase-inhibitor activity of full-length Ha-ras oncogene products by denaturation-renaturation.
abstract: We have investigated protease-inhibitory activity against cathepsin L of human and murine Ha-ras oncogene products (p21s) produced by Escherichia coli. The inhibitory activity of full-length p21s was much weaker than that of truncated p21s, however, the inhibitory activity was potentiated after denaturation with 8 M urea and 2 M NaCl followed by renaturation. These suggest that p21 can be folded into multiple three-dimensional conformations which have different protease-inhibitory activities.
authors.affiliation: Division of Biochemistry, Chiba Cancer Center Research Institute, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Hiwasa
authors.forename: S
authors.initials: S
authors.lastname: Yokoyama
authors.forename: J
authors.initials: J
authors.lastname: Fujita
authors.forename: E
authors.initials: E
authors.lastname: Kominami
authors.forename: N
authors.initials: N
authors.lastname: Katunuma
authors.forename: S
authors.initials: S
authors.lastname: Sakiyama
mesh_terms: D000818:Animals; D056668:Cathepsin L; D002403:Cathepsins / Q000037:antagonists & inhibitors; D003546:Cysteine Endopeptidases; D015853:Cysteine Proteinase Inhibitors; D010450:Endopeptidases; D006801:Humans; D015689:Oncogene Protein p21(ras) / Q000502:physiology*; D011489:Protein Denaturation; D051381:Rats
chemical_list: D015853:Cysteine Proteinase Inhibitors; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; C534281:CTSL protein, human; D056668:Cathepsin L; C534280:Ctsl protein, rat; D015689:Oncogene Protein p21(ras)