α‐キモトリプシンを作用させた絹フィブロインの構造
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- 塚田 益裕
- 農林水産省蚕糸試験場
書誌事項
- タイトル別名
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- Effect of .ALPHA.-chymotrypsin on the structure of silk fibroin.
- アルファ キモトリプシン オ サヨウサセタ キヌ フィブロイシ ノ コウゾウ
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説明
Structure of the chymotrypsin-resistant fraction from regenerated (solubilized) silk fibroin (Fli·cp) and native silk fibroin (FN·cp) was studied by infrared spectroscopy, x-ray diffractometry, scanning electron microscopy and DSC measurement.<br>On the basis of the infrared spectra and x-ray diffraction micrographs, it was found that chymotrypsin-resistant Fli·cp and FN·cp exhibited the silks and silk I crystalline form, respectively, suggesting that the crystalline structure of silk fibroin differed markedly as a result of the change of the specimen's preparation. The thermal decomposition temperature of Fli·cp shifted to a higher temperature compared to that of the coagulated silk fibroin with a silk II crystalline form, depending largely on the presence of highly organized crystallite and the removal of the random coil region resulting from the action of chymotrypsin. Scanning electron micrographs of Fli·cp revealed a granular form (0.3μm in diameter), differing significantly from that for FN·cp.
収録刊行物
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- 日本蚕糸学雑誌
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日本蚕糸学雑誌 55 (2), 126-130, 1986
社団法人 日本蚕糸学会
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詳細情報 詳細情報について
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- CRID
- 1390282679506314368
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- NII論文ID
- 130004030829
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- NII書誌ID
- AN00190300
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- ISSN
- 1884796X
- 00372455
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- NDL書誌ID
- 3082352
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- IRDB
- NDL
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可