Purification and Characterization of Chymotrypsin Inhibitor CI-3 from Hemolymph of Silkworm,Bombyx mori

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The chymotrypsin inhibitor 3 (Cl-3) whose expression is controlled by Ict-E gene on the 22nd linlage group was purified from the larval hemolymph of silkworm Bombyx mori by combination of series of column chromatography and polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE). The molecular weight of Cl-3 was 40kDa and its isoelectic point was 5.5. The results of analysis on the protein propeties revealed that the inhibitory activity of Cl-3 against α-chymotrypsin was remarlably stable at pH 5.9 and pH 11.9, respectively. Cl-3 was quite stable at the temperature between 0℃ to 50℃ and lost inhibitory activity completely at the temperatures higher than 60℃. Cl-3 showed inhibitory activity toward α-chymotrypsin and silkworm digestive juice(DJ) protease.
九州大学の論文