Purification and Characteristics of Diamine Oxidase from the Apoplast of Pea Epicotyls

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概要

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• Diamine oxidase was solubilized by stirring with a buffer from the apoplast of pea epicotyls and purified to homogeneity by one-step technique. The specific activity of the purified diamine oxidase was 22.5U/mg protein. SDS gel electrophoresis showed a single band at a molecular weight of 70KDa（1%SDS and 5%mercaptoethanol, at100℃ for10min）and main band at a molecular weight of 140KDa（1% SDS only, at 100℃ for10min). The enzyme activity was inhibited strongly by carbonyl reagents but was little inhibited by chelaters. The effect of the copper addition was not admitted at all.

• 愛知教育大学の論文
• 2009-03-01

著者

• 柳澤 寛

  Department Of Biology Aichi University Of Education

関連論文

• Techniques for the separation of proteins by isoelectric point column chromatography
• Purification and Characteristics of Diamine Oxidase from the Apoplast of Pea Epicotyls

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