Diamine oxidase from Lens esculenta seedlings: purification and properties
G Floris, A Giartosio, A Rinaldi
Index: Floris, Giovanni; Giartosio, Anna; Rinaldi, Augusto Phytochemistry (Elsevier), 1983 , vol. 22, # 9 p. 1871 - 1874
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Citation Number: 81
Abstract
Abstract A diamine oxidase (DAO)(EC 1.4. 3.6) has been purified to homogeneity from lentil seedlings. The purified protein has a MW of 154 000 and is composed of two apparently identical subunits. It contains two CU 2+ atoms and one carbonyl-like group per mol. The purified enzyme is pink-red in concentrated solution and shows a broad, well-defined, absorption band in the visible region centered at 498 nm. The ESR spectrum is typical of ...
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