Purification and characterization of a chymotrypsin inhibitor with an oligosaccharide chain from the hemolymph of Bombyx mori.
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The chymotrypsin inhibitor CI-8 whose expression is controlled by the Ict-D gene was purified from the larval hemolymph of Bombyx mori by a series of chromatography using DEAE-Sepharose, Con A-Agarose and Butyl-Toyopearl. CI-8 was a protein with a pI of 5.0 and a molecular weight of 42, 000. This inhibitor was found to contain an oligosaccharide chain. The inhibitory activity of CI-8 decreased under acidic conditions while it was remarkably stable under alkaline conditions. Its activity completely lost at 65°C at pH 7.0 CI-8 strongly inhibited bovine pancreatic chymotrypsin and B. mori digestive protease and also weakly a protease from Beauveria bassiana, which is a fungus pathogenic to B. mori. The antiserum raised against CI-8 reacted to the chymotrypsin inhibitors CIs-6 and 7 controlled also by the allelic genes of the Ict-D locus but not with other chymotrypsin inhibitors controlled by the Ict-A, Ict-B, Ict-E and Ict-H genes.
- 社団法人 日本蚕糸学会の論文
社団法人 日本蚕糸学会 | 論文
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