Trypsin及びPepsinのPeriodateによる酸化

• 資料種別: 記事
• タイトル: Trypsin及びPepsinのPeriodateによる酸化
• 著者・編者: 前川 一之 他
• 著者標目: 前川 一之
• タイトル（掲載誌）: 日本農芸化学会誌 : 生命・食糧・環境
• 巻号年月日等（掲載誌）: 30(4) 1956.04
• 掲載巻: 30
• 掲載号: 4
• 掲載ページ: ????
• 掲載年月日（W3CDTF）: 1956-04
• ISSN（掲載誌）: 0002-1407
• ISSN-L（掲載誌）: 0002-1407
• 出版事項（掲載誌）: 東京 : 日本農芸化学会
• 出版地（国名コード）: JP
• 本文の言語コード: jpn
• NDLC: ZR7
• 対象利用者: 一般
• 所蔵機関: 国立国会図書館
• 請求記号: Z18-335
• 連携機関・データベース: 国立国会図書館 : 国立国会図書館雑誌記事索引; https://ndlsearch.ndl.go.jp
• 書誌ID（NDLBibID）: 10061367; http://id.ndl.go.jp/bib/10061367
• 整理区分コード: 632

• 要約等: 1) As trypsin was oxidized by sodium meta-periodate, the enzymatic activity diminished during the process of the reaction. After oxidizing for 2 hrs. at 5°, the oxidized trypsin which kept 91% of the original activity was obtained in crystalline form.<br> 2) The optimum pH for proteolytic activities of trypsin and pepsin shifted toward neutral after periodate oxidation.<br> 3) The optimum pH for proteolytic activities of trypsin and pepsin shifted toward neutral after periodate oxidation.<br> 3) Trypsin which was after oxidized for 45 hours consumed 42 moles of periodate per mole of enzyme and the activity diminished to 40% using hemoglobin and casein as substrates. As compared with pepsin, trypsin consumed slowly but more oxidants per mole of enzyme, but the decrease in tryptic activity was far less.<br> 4) In case of gelatin liquefaction it was found that diminution of tryptic and peptic activity was markedly different from the above-mentioned facts, i. e. pepsin retained 51% of gelatin liquefying activity after oxidation for 45 hrs, whereas trypsin retained only 5% after same period.<br> Considering together the above-mentioned fact and the tendency of consuming NaIO₄, it is deduced that trypsin possesses more groups which are slowly oxidized than pepsin and that these groups may contribute to the gelation liquefaction.
• DOI: 10.1271/nogeikagaku1924.30.4_183
• オンライン閲覧公開範囲: インターネット公開
• 連携機関・データベース: 科学技術振興機構 : J-STAGE; http://www.jstage.jst.go.jp

• 要約等: 1) As trypsin was oxidized by sodium meta-periodate, the enzymatic activity diminished during the process of the reaction. After oxidizing for 2 hrs. at 5°, the oxidized trypsin which kept 91% of the original activity was obtained in crystalline form.<br> 2) The optimum pH for proteolytic activities of trypsin and pepsin shifted toward neutral after periodate oxidation.<br> 3) The optimum pH for proteolytic activities of trypsin and pepsin shifted toward neutral after periodate oxidation.<br> 3) Trypsin which was after oxidized for 45 hours consumed 42 moles of periodate per mole of enzyme and the activity diminished to 40% using hemoglobin and casein as substrates. As compared with pepsin, trypsin consumed slowly but more oxidants per mole of enzyme, but the decrease in tryptic activity was far less.<br> 4) In case of gelatin liquefaction it was found that diminution of tryptic and peptic activity was markedly different from the above-mentioned facts, i. e. pepsin retained 51% of gelatin liquefying activity after oxidation for 45 hrs, whereas trypsin retained only 5% after same period.<br> Considering together the above-mentioned fact and the tendency of consuming NaIO₄, it is deduced that trypsin possesses more groups which are slowly oxidized than pepsin and that these groups may contribute to the gelation liquefaction.
• DOI: 10.1271/nogeikagaku1924.30.4_183; https://doi.org/10.1271/nogeikagaku1924.30.4_183
• 関連情報（URI）: http://id.ndl.go.jp/bib/10061367; https://ndlsearch.ndl.go.jp/books/R000000004-I10061367
• 連携機関・データベース: 国立情報学研究所 : CiNii Research; https://cir.nii.ac.jp/
• 提供元機関・データベース: Japan Link Center; https://japanlinkcenter.org/top; 雑誌記事索引データベース; https://ndlsearch.ndl.go.jp; Crossref; https://www.crossref.org; CiNii Articles
• 書誌ID（NDLBibID）: 10061367; http://id.ndl.go.jp/bib/10061367
• NII論文ID: 130001215204