@article{oai:aue.repo.nii.ac.jp:00000653,
 author = {Sakakibara, Yoko and Yanagisawa, Hiroshi},
 journal = {愛知教育大学研究報告, 自然科学編},
 month = {Mar},
 note = {text, 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.},
 pages = {61--64},
 title = {Purification and Characteristics of Diamine Oxidase from the Apoplast of Pea Epicotyls},
 volume = {58},
 year = {2009}
}