Ｐｈａｇｅ　ｃｏａｔたんぱく質に関する研究　Ｉ　　第３分画（Ｆ３）の分子構造について

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タイトル別名
  • STUDIES ON PHAGE COAT PROTEIN
  • Phage coat protein ニカンスルケンキュウ 1 ダイ 3 ブン
  • I. 第3分画 (F3) の分子構造について

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抄録

The proteins of Salmonella phage P22 were extracted with acetic acid and fractionated on a DEAE-cellulose column. The fractionated proteins were named Fraction 1 (F1), Fraction 2 (F2) and Fraction 3 (F3). F3 protein was suggested to be a main component related to the production of antibody. It was investigated for biochemical characteristics.<br>1. When P22 protein (P22P) was fractionated on a DEAE-cellulose column with 0.001-0.02M phosphate buffer, a large yield was obtained after the pH of the sample was regulated with 0.001M phosphate buffer before fractionation.<br>2. The isolated F3 fraction was treated with trypsin and developed by two-dimensional paper chromatography. Sixteen peptides were detected with ninhydrin solution.<br>3. The N-terminal amino acid sequence of the fraction was determined by the dansyl method. It was suggested that the N-terminal might be the Val-Val or Val-Ile sequence.<br>4. After citraconylation and tryptic digestion, the fraction was applied to Dowex 50X2 with pyridinium acetate buffer. By the fluorescamine method 9-18 peaks were detected. With 10 of these peaks the N-terminal sequence was determined by the dansyl method.

収録刊行物

  • ウイルス

    ウイルス 29 (2), 141-148, 1979

    日本ウイルス学会

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