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きびアルコール可溶性蛋白質の構成ポリペプチド(B. 生活科学)
https://kpu.repo.nii.ac.jp/records/5323
https://kpu.repo.nii.ac.jp/records/5323c8ffec34-6ef2-40b9-a14c-cafd7b19def1
名前 / ファイル | ライセンス | アクション |
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KJ00000079449.pdf (567.0 kB)
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Item type | [ELS]紀要論文 / Departmental Bulletin Paper(1) | |||||
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公開日 | 2017-02-20 | |||||
タイトル | ||||||
言語 | ja | |||||
タイトル | きびアルコール可溶性蛋白質の構成ポリペプチド(B. 生活科学) | |||||
その他(別言語等) | ||||||
その他のタイトル | Component Polypeptides of Alcohol-Soluble Protein from Proso Millet (B. LIVING SCIENCE) | |||||
言語 | en | |||||
言語 | ||||||
言語 | jpn | |||||
資源タイプ | ||||||
資源タイプ | departmental bulletin paper | |||||
著者 |
牧, 善輔
× 牧, 善輔× 田代, 操 |
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抄録(日) | ||||||
内容記述タイプ | Other | |||||
内容記述 | 70%アルコール抽出により, きびからアルコール可溶性蛋白質が得られた.本蛋白質はSephadex G-100でのゲル濾過によりF-1からF-4の4画分に分離され, その内分子量約10万以上に相当するF-1,分子量約4万から10万に相当するF-2が主要画分であると示された.一方, アルコール可溶性蛋白質を還元さらにS-シアノエチル化した後, 同様にゲル濾過を行なうと, 先のF-1に相当する画分が消失しF-2に相当する画分が増加した.アミノ酸分析からは, F-1,F-2の組成は全んど同一であることが示された.非還元系でのSDS-ゲル電気泳動では, アルコール可溶性蛋白質は主にポリペプチドとして分子量4万と2万の両者, F-1は分子量4万, F-2は分子量2万のものを示した.さらにこれらを還元S-シアノエチル化した場合, その電気泳動パターンは皆同一となり, 分子量2万を与えるポリペプチドの主バンドのみとなった.以上の結果より, きびアルコール可溶性蛋白質は基本単位として分子量2万のポリペプチドを有し, これがSS結合や疎水結合等によりさまざまに分子量を異にするポリペプチド会合体を構成していると結論できる. | |||||
言語 | ja | |||||
抄録(英) | ||||||
内容記述タイプ | Other | |||||
内容記述 | The alcohol-soluble protein from proso millet was prepared by extraction with 70% ethanol. This protein was fractionated into four fractions, F-1,F-2,F-3 and F-4 by gel filtration on Sephadex G-100,and F-1 having the molecular weight of more than 100,000 and F-2 having that of between 40,000-100,000 were shown to be main fractions. On the other hand, the gel filtration profile of the reduced and S-cyanoethylated protein showed that the F-1 fraction disappeared and the F-2 fraction increased. The amino acid composition of F-1 was almost identical with that of F-2. Further, SDS-polyacrylamide gel electrophoresis indicated that the reduced and S-cyanoethylated alcohol-soluble protein, F-1 and F-2 gave the same electrophoretic patterns which had the single main polypeptide band corresponding to the molecular weight of 20,000. These results suggested that the alcohol-soluble protein from proso millet was composed of the polymers of the primary polypeptide chain having the molecular weight of 20,000. | |||||
言語 | en | |||||
書誌情報 |
ja : 京都府立大学学術報告. 理学・生活科学 en : The scientific reports of the Kyoto Prefectural University. Natural science and living science 巻 29, p. 21-25, 発行日 1978-11-30 |
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雑誌書誌ID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AN00062300 | |||||
ISSN | ||||||
収録物識別子タイプ | PISSN | |||||
収録物識別子 | 0075739X |