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  • 1
    ISSN: 1432-2048
    Keywords: Diamine oxidase ; H2O2 synthesis (cell wall) ; Lens (polyamine levels) ; Pisum (polyamine levels) ; Polyamine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Diamine-oxidase (DAO; EC 1.4.3.6) activity and di-and polyamine levels were estimated along the epicotyl and root of light-grown and etiolated lentil (Lens culinaris Medicus) and pea (Pisum sativum L.) seedlings. The activity of DAO was higher in etiolated epicotyls than in lightgrown ones. In both species there was a positive correlation between DAO activity and the diamine (putrescine and cadaverine) levels along the whole epicotyl and root. Polyamine (spermine and spermidine) distribution seemed to be associated with the meristematic and elongating zone of the epicotyl and root. The physiological function of DAO is discussed in relation to its possible role in providing hydrogen peroxide to peroxidase-dependent reactions occurring in the cell wall.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Injury (by cutting, K+ uptake) ; Oxidase (diamine, polyamine) ; Pisum (K+ uptake) ; Polyamine ; Potassium uptake (plasma membrane) ; Root (injury, K+ uptake) ; Zea (K+ uptake)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The inhibition of K+ uptake through the plasma membrane resulting from injury caused by cutting, or from application of polyamines (PAs), has been investigated in root segments of maize (Zea mays L.) and pea (Pisum sativum L.). It was found, for both treatments, that K+ uptake recovered if the segments were washed for 2 h. The K+ uptake inhibited by cutting and that inhibited by spermidine treatment were stimulated to the same extent by fusicoccin. In addition, there was a correlation between the extent of the recovery of K+ uptake caused by washing and the distribution, along the root axis, of both PAs and the activities of enzymes responsible for PA degradation. In apical segments of maize, where the PA content and the activity of the degradative enzyme polyamine oxidase (EC 1.5.3.3) were higher than in the more distal segments, the recovery of K+ uptake caused by washing was also higher. On the other hand, the opposite trend was observed in root segments of pea, where the PA content and the activity of the degradative enzyme diamine oxidase (EC 1.4.3.6) were higher in distal segments in which K+ uptake was greatly stimulated by washing. The effect of the amine-oxidase inhibitor, aminoguanidine, indicates that the degradation products of PAs are involved in the mechanism of inhibition of K+ uptake by PAs. The data also seem to indicate that PAs and their degradation products are responsible for the inhibition of K+ uptake occurring as a result of injury sustained by cutting roots into segments.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Planta 167 (1986), S. 300-302 
    ISSN: 1432-2048
    Keywords: Diamine oxidase ; Extracellular solution ; Hydrogen peroxide production ; Pisum (diamine oxidase)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Most of the diamine oxidase (EC 1.4.3.6) present in pea (Pisum sativum L. cv. Rondo) epicotyls is found in the fluid obtained by centrifuging pea epicotyl sections previously infiltrated under vacuum with a buffer solution. No detectable amount of the cytoplasmic enzyme glucose-6-phosphate dehydrogenase is present in this fluid, showing that there is very little contamination by cell contents. Polyacrylamide-gel electrophoresis and specific-activity data indicate that diamine oxidase is the most plentiful protein in the extracellular solution obtained from pea epicotyl sections and that an active process is involved in the selective transfer of the enzyme outside the cell. The possible involvement of diamine oxidase in the supply of H2O2 to peroxidase-catalyzed reactions occurring inside the cell wall is discussed.
    Type of Medium: Electronic Resource
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