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Purification and some properties of an amine oxidase from soybean seedlings
Authors:I Nikolov  V Pavlov  I Minkov  D Damjanov
Institution:(1) Biological Faculty, Sofia University, 1421 Sofia, (Bulgaria);(2) Oncological Research Institute, Medical Academy, 1156 Sofia, (Bulgaria)
Abstract:Summary An amine oxidase was purified 447-fold from soybean seedlings and some of its properties were investigated. The molecular weight of the enzyme was estimated to be 25,000. It was most active towards putrescine, followed by spermidine and spermine. Km-values for these substrates were relatively close. The enzyme was strongly inhibited by carbonyl reagents, such as semicarbazide and aminoguanidine.
Keywords:Glycine max  soybean seedlings  amine oxidase  putrescine  spermidine  spermine
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