• Title/Summary/Keyword: Arismatis Rhizoma trypsin inhibitor(ARTI)

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Purification and Characterization of Trypsin Inhibitor from Alismatis Rhizoma (택사(Alismatis Rhizoma) trypsin inhibitor의 정제와 특성)

  • 박종옥;이인섭
    • Journal of Life Science
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    • v.12 no.2
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    • pp.151-157
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    • 2002
  • A trypsin inhibitor was isolated and purified from Azismatis Rhizoma which has been used as a galenic for diuretic and antiphlogistic. Purification was carried out by 0-80% saturated ammonium sulfate salting out, DEAE- cellulose ion exchange chromatogrphy, Sephadex G-150 gel filtration. The molecular weight of Alismatis Rhizoma trypsin inhibitor(ARTI) was estimated to be about 23,000 Da by gel filtration and SDS-PAGE, it must be monomer. ARTI was stable at 0~6$0^{\circ}C$, but at higher temperature its activity was decreased about 35%. When benzoyl-dl-arginine p-nitroanilide was used as a substrate of trypsin, half-maximal inhibition of ARTI was observed at 0.071 $\mu$M. ARTI inhibited the hydrolysis of trypsin non-competitively and Km value was 0.81 $\mu$M.