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KMID : 0613820020120020151
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Journal of Life Science
2002 Volume.12 No. 2 p.151 ~ p.157
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Purification and Characterization of Trypsin Inhibitor from Alismatis Rhizoma
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Park Jong-Ok
Lee In-Sub
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Abstract
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A trypsin inhibitor was isolated and purified from Alismatis 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 0～60℃, 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 0.071μM. ARTI inhibited the hydrolysis of trypsin non-competitively and Km value was 0.81μM
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KEYWORD
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Alismatis Rhizoma, trypsin inhibitor, Alismatis Rhizoma trypsin inhibitor(ARTI)
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