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KMID : 0380619940260010081
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Korean Journal of Food Science and Technology
1994 Volume.26 No. 1 p.81 ~ p.87
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Characterization of Trypsin Inhibitors Purified from Trichosanthes kirilowii Root
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김희숙/Kim, Hee Sook
박은주/윤두희/조은정/류병호/Park, Eun Ju/Yun, Doo Hee/Cho, Eun Jung/Ryu, Byung Hho
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Abstract
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Two different trypsin inhibitors, TRTI-1 and TRTI-2, were purified to near homogenity from Trichosanthes kirilowii root, by 0∼90% saturated ammonium sulfate salting out, DEAE-Sephacel ion exchange chromatography, Sephadex G-50 gel filtration chromatography and trypsin-affinity chromatography. The molecular weight of TRTI-1 and TRTI-2 were estimated to be about 5,000 Da and 24,000 Da, respectively, by gel filtration and must be monomer and homodimer since they contain 4,000 Da and 10,000 Da each on SDS-polyacrylamide gel electrophoresis. TRTI-1 was stable after heating for at least 2 hr at 100C but TRTI-2 was completely inactivated after heating for 10 min at 90℃ . When Bz-dlArg-pNA was used as a substrate of TPCK-treated trypsin, half-maximal inhibitions of TRTI-1 and TRTI-2 were observed at 0.8 wM and 6 PM, repectively. Both TRTI-1 and TRTI-2 inhibited the hydrolysis of trypsin competitively and Km values were 0.97 pM and 0.63 PM, respectively. Both TRTI1 and TRTI-2 specifically inhibited trypsin but they did not inhibit other proteases tested, chymotrypsin, papain, elastase, collagenase, thermolysin, Nagarase, pepsin, and thrombin.
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KEYWORD
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