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KMID : 0370220080520010079
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Yakhak Hoeji
2008 Volume.52 No. 1 p.79 ~ p.84
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Purification and Characterization of Trypsin Inhibitor from Alismatis Rhizoma and its Binding Protein, 10-Formyltetrahydrofolate Dehydrogenase
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Kim Ji-Man
Park Jong-Ok
Shin Young-Hee
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Abstract
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Alismatis Rhizoma has been used as diuretics and antiphlogistics in the Chinese oriental medicine. A trypsin inhibitor was isolated from Alismatis Rhizoma using DEAE ion exchange column, trypsin affinity column, and FPLC chromatography, and its activity and characteristics were studied. The purifed Alismatis Rhizoma trypsin inhibitor (ARTI) was estimated to be about 22 kDa. The sequence determination on N-terminal amino acid residues and 84 amino acid residues has been completed, yet no homology has been found with trypsin inhibitors reported at NCBI. ARTI did not show inhibitory activities on chymotrypsin and elastase, however it exhibited a significant inhibitory activity on bovine trypsin, and formed a complex with rat liver 10-formyltetrahydrofolate dehydrogenase.
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KEYWORD
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Alsmatis Rhizoma trypsin inhibitor (ARTI), Partial amino acid sequence, ARTI-affinity column, 10-formyltetrahydrofolate dehydrogenase (FDH)
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