Tomato Peroxidase: Purification by Affinity Chromatography

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概要

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• The glycoprotein nature of soluble peroxidase isolated from the tomato fruit was established using Schiffs reagent after periodic oxidation. This enzyme retained on a concanavalin A Sepharose column was eluted using an α-methyl-D-mannoside gradient. On including this step in the purification scheme, the tomato peroxidase was purified 263-fold with a yield of 63%. The enzyme so obtained was homogeneous on polyacrylamide gel electrophoresis and its RZ value was 2.8.

• 社団法人 日本農芸化学会の論文

著者

• CROUZET Jean

  Centre de Génie Technologie Alimentaires, Laboratoire de Biochimie Appliquée, Université des Sciences et Techniques du Languedoc

• SIGNORET Alice

  Centre de Génie Technologie Alimentaires, Laboratoire de Biochimie Appliquée, Université des Sciences et Techniques du Languedoc

関連論文

• Tomato Peroxidase: Purification by Affinity Chromatography

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