Diamine oxidase from Lens esculenta seedlings: Purification and properties
1983; Elsevier BV; Volume: 22; Issue: 9 Linguagem: Inglês
10.1016/0031-9422(83)80004-1
ISSN1873-3700
AutoresGiovanni Floris, Anna Giartosio, Andrea Rinaldi,
Tópico(s)Enzyme-mediated dye degradation
ResumoA 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 CU2+ 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 Cu2+ in a tetragonal symmetry. The enzyme oxidizes only aliphatic diamines and spermidine with formation of the corresponding aldehydes, hydrogen peroxide and ammonia. Putrescine and cadaverine are oxidized most rapidly and the oxidation rate decreases when longer diamines are tested.
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