Selective Oxidation of Tryptophan and Histidine Residues in Protein through the Copper-catalyzed Autoxidation of _L-Ascorbic Acid(Food & Nutrition)

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概要

• 論文の詳細を見る

• The oxidative modification of bovine serum albumin with an ascorbic acid-copper ion system was studied. Under physiological conditions (pH 7.2, ambient temperature), this system mainly caused the modification of amino acid residues in the protein, and its polymerization was scarcely observed. The results of spectrophotometric assays and amino and analysis of the protein clearly suggested the selective damage to tryptophan and histidine residues. The reaction could be retarded by catalase and Cu(II)-chelating agents, while superoxide dismutase and hydroxyl radical scavengers showed little effect. These specific reactions were explained by the site-specific formation of the oxygen-derived free radical followed by its reaction with a specific site of the protein.

• 社団法人日本農芸化学会の論文
• 1988-06-23

著者

• UCHIDA KOJI

  Department of Respiratory Medicine, Juntendo University School of Medicine

• KAWAKISHI Shunro

  Department of Food Science and Technology, Nagoya University

• Uchida Koji

  Department Of Food Science & Technology Nagoya University

• Uchida Koji

  Department Of Food Science And Technology Nagoya University

• Kawakishi Shunro

  Department Of Food And Nutrition Sugiyama Jogakuen University

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