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Iodination of Ricin D
Authors:Masatsune Ishiguro  Etsuko Taira  Kazuto Mashima  Gunki Funatsu  Masaru Funatsu  Motosuke Kikutani
Institution:1. Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Hakozaki, Higashi-ku, Fukuoka 812;2. Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Nagasaki University, 1–14 Bunkyo-machi, Nagasaki 852
Abstract:Approximately five tyrosine residues of ricin D were iodinated preferentially under appropriate conditions probably forming diiodotyrosine. Iodination of this toxin carried out in 0.1 m phosphate buffer at pH 7.0 and 0°C for 60 min with a 20 fold molar excess of iodine per mole of protein, yielded a main component which appeared as a single band on polyacrylamide gel disc electrophoresis. Analysis of protein-bound radioactivity and the content of diiodotyrosine of 181I-labeled ricin D revealed that two tyrosine residues in the isoleucyl chain and three in the alanyl chain were substituted. The toxicity of iodinated ricin D decreased to one hundredth of that of native protein, However, the hemagglutinating activity of this protein was not affected by the iodination reaction.
Keywords:family-19 chitinase  chitin-binding domain  protoplast
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