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http://dx.doi.org/10.5352/JLS.2002.12.2.151

Purification and Characterization of Trypsin Inhibitor from Alismatis Rhizoma  

박종옥 (경성대학교 화학과)
이인섭 (경성대학교 생물학과)
Publication Information
Journal of Life Science / v.12, no.2, 2002 , pp. 151-157 More about this Journal
Abstract
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.
Keywords
Alismatis Rhizoma; trypsin inhibitor; Arismatis Rhizoma trypsin inhibitor(ARTI);
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