Sweet potato (Ipomoea batatas (L.) Lam) trypsin inhibitors, the major root storage proteins, inhibit one endogenous serine protease activity

Wen C. Hou, Yaw Huei Lin

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)733-739
Number of pages7
JournalPlant Science
Volume163
Issue number4
DOIs
Publication statusPublished - Oct 1 2002

Fingerprint

Ipomoea batatas
Trypsin Inhibitors
Serine Proteases
serine proteinases
trypsin inhibitors
storage proteins
sweet potatoes
Sepharose
agarose
arginine
Arginine
Proteins
proteinases
Aprotinin
Complex Mixtures
Soybeans
Edetic Acid
Trypsin
serine
trypsin

Keywords

  • Physiological function
  • Regulation
  • Serine protease
  • Sweet potato
  • Trypsin inhibitor

ASJC Scopus subject areas

  • Plant Science
  • Biochemistry
  • Biotechnology

Cite this

Sweet potato (Ipomoea batatas (L.) Lam) trypsin inhibitors, the major root storage proteins, inhibit one endogenous serine protease activity. / Hou, Wen C.; Lin, Yaw Huei.

In: Plant Science, Vol. 163, No. 4, 01.10.2002, p. 733-739.

Research output: Contribution to journalArticle

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