FEBS Letters | |
v‐Ha‐Ras insertion/deletion mutants with reduced protease‐inhibitory activity have no transforming activity | |
Sakiyama, Shigeru1  Sawada, Toshie1  Hiwasa, Takaki1  | |
[1] Division of Biochemistry, Chiba Cancer Center Research Institute, 666-2 Nitona-cho, Chuo-ku, Chiba 260, Japan | |
关键词: v-Ha-ras; Oncogene product; Protease inhibitor; Cathepsin; GTP binding; DTT; dithiothreitol; E. coli; Escherichia coli; GAP; GTPase activating protein; MES; 2-(N-morpholino)ethanesulfonic acid; Ras; ras oncogene product; Z-Arg-Arg-MCA; 7-(benzyloxycarbonyl-arginyl-arginyl-amino)-4-methylcoumarin; Z-Phe-Arg-MCA; 7-(benzyloxycarbonyl-phenylalanyl-arginyl-amino)-4-methylcoumarin; | |
DOI : 10.1016/0014-5793(93)80532-Y | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
We have purified 26 insertion/deletion mutants of v-Ha-ras oncogene products produced by Escherichia coli and investigated their protease-inhibitory activity toward papain and cathepsins B and L. K i values for papain were relatively similar among the mutants, however, those for cathepsins B and L varied up to 10-fold. Among them, four mutants, 1–48 LIR 54–189, 1–110 LIS 112–189, 1–130 PDQ 146–189 and 1–155 LIR 166–189, showed significant reduction in the inhibitory activity toward cathepsin L and these four mutants have lost transforming activity toward NIH3T3 mouse fibroblasts. However, some other mutants also showed no transforming activity in spite of possession of the potent protease-inhibitory activity, suggesting that the protease-inhibitory activity of Ras might be necessary but not sufficient for its biological activity.
【 授权许可】
Unknown
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