Isolation and properties of two allelic chymotrypsin inhibitors from the hemolymph of the silkworm,Bombyx mori |
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| Institution: | 1. Center for iPS Cell Research and Application (CiRA), Kyoto University, 53 Kawahara-cho, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan;2. Department of Diabetes and Clinical Nutrition, Graduate School of Medicine, Kyoto University, 54 Kawahara-cho, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan;3. Department of Clinical Research, National Hospital Organization, Nagara Medical Center, 1300-7 Nagara, Gifu 502-0071, Japan;4. Department of Metabolic Medicine, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita 565-0871, Japan |
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| Abstract: | A chymotrypsin inhibitor, CI-1, and its co-dominant allelic counterpart CI-2, detectable in certain strains of Bombyx mori each as an electrophoretic band close to the origin, were purified from the larval hemolymph by using ion-exchange and affinity chromatography. CIs 1 and 2 were monomeric neutral proteins with a pI of 7.12 and 7.00 and an Mr of about 10,400 and 7900, respectively. Amino acid analysis showed that these inhibitors were rich in aspartic acid (or asparagine), glutamic acid (or glutamine) and lysine, but poor, or lacking, in valine, methionine, histidine and arginine. In the amino-terminal sequence, 14 out of 20 amino acid residues analyzed were common between CIs 1 and 2. |
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