Potentiation of cysteine proteinase-inhibitor activity of full-length Ha-ras oncogene products by denaturation-renaturation.
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.
Hiwasa
T
T
Division of Biochemistry, Chiba Cancer Center Research Institute, Japan.
Yokoyama
S
S
Fujita
J
J
Kominami
E
E
Katunuma
N
N
Sakiyama
S
S
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
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)