摘要
Proteases were purified successively by trypsin-Sepharose 4B, sweet potato (Ipomoea batatas [L.] Lam) trypsin inhibitor (SPTI)-Sepharose 4B, benzamidine-Sepharose 6B, and arginine-Sepharose 4B affinity columns from crude extracts of SP dormant roots. One of them, Arg-1, was specific to the substrate benzoyl-arginine-p-nitroanilide, with an optimal pH 8.0. Arg-1 migrated as a single band of 20 kDa in SDS-PAGE, detected by activity staining. The activity was completely inhibited by SPTI in a dose-dependent manner. The activity was inhibited by aprotinin and soybean TI, but not by E-64, pepstatin A or EDTA. This suggested that Arg-1 was a serine type protease, inhibited endogenously by SPTI. Denatured SPTI could be degraded by Arg-1 in vitro. The physiological role of SPTI in the regulation of Arg-1 activity was discussed.
原文 | 英語 |
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頁(從 - 到) | 733-739 |
頁數 | 7 |
期刊 | Plant Science |
卷 | 163 |
發行號 | 4 |
DOIs | |
出版狀態 | 已發佈 - 10月 1 2002 |
ASJC Scopus subject areas
- 植物科學
- 生物化學
- 生物技術