Glutathione peroxidase-like activity of 33 kDa trypsin inhibitor from roots of sweet potato (Ipomoea batatas [L.] Lam 'Tainong 57')

Wen C. Hou, Hsien Jung Chen, Chuan Hsiao Han, Ching Yang Lin, Yaw Huei Lin

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14 Citations (Scopus)


The hydrogen peroxide, glutathione (GSH), 3-(4,5-dimethylthiazol-2-yl)-2,5- diphenyltetrazolium bromide (MTT) and phenazine methosulfate (PMS) were used for spectrophotometric assay of commercial glutathione peroxidase (GPx) activity at 570nm. A positive correlation (r2=0.998) was found between level of GPx activity and the absorbance changes (%). The 33kDa trypsin inhibitor (TI) was purified from the storage roots of sweet potato (SP) (Ipomoea batatas [L.] Lam 'Tainong 57') by trypsin-Sepharose 4B affinity chromatography and preparative acrylamide gel electrophoresis. The first 15 amino acids in the N-ternimal region of 33kDa TI were SSETPVLDINGDEVR, which were identical to that of deduced sequence of sopramin A or B. A positive correlation (r 2=0.979) was found between the amounts of 33kDa TI added and absorbance changes. Absorbance changes of 5.18, 16.35 and 25.83%, respectively, were obtained when 100, 200 and 250μg 33kDa TI were added, which were equal to 0.56, 1.21 and 1.76 GPx units. Using TI and GPx activity stainings, it was confirmed that 33kDa TI exhibited GPx-like activity. The physiological significance of TIs with GPx activities is discussed.

Original languageEnglish
Pages (from-to)1541-1546
Number of pages6
JournalPlant Science
Issue number6
Publication statusPublished - Jun 2004


  • Ammonium persulfate
  • APS
  • Bis
  • CBG
  • Commassie brilliant blue G-250
  • Glutathione
  • Glutathione peroxidase
  • GPx
  • GSH
  • N,N′-methylenediacrylamide
  • Sodium dodecylsulfate-polyacrylamide gel electrophoresis
  • SP
  • Sweet potato

ASJC Scopus subject areas

  • Plant Science
  • Biochemistry
  • Biotechnology


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