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melilotus officinalis/oxidase
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Comparison of kinetic properties of amine oxidases from sainfoin and lentil and immunochemical characterization of copper/quinoprotein amine oxidases.
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Kinetic properties of novel amine oxidase isolated from sainfoin (Onobrychis viciifolia) were compared to those of typical plant amine oxidase (EC 1.4.3.6) from lentil (Lens culinaris). The amine oxidase from sainfoin was active toward substrates, such as 1,5-diaminopentane (cadaverine) with K(m) of
Isolation of Tricin as a Xanthine Oxidase Inhibitor from Sweet White Clover (Melilotus albus) and Its Distribution in Selected Gramineae Species.
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Xanthine oxidase, an enzyme present in significant levels in the intestine and liver, metabolizes hypoxanthine to xanthine and xanthine to uric acid in the purine catabolic pathway. An inhibitory compound acting against xanthine oxidase was isolated from sweet white clover (Melilotus albus) by
Hydrogen peroxide-dependent antibacterial action of Melilotus albus honey.
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Honey originating from different floral sources exhibits the broad spectrum of antibacterial activity as a result of the presence of hydrogen peroxide as well as nonperoxide bioactive compounds. The mechanisms of antibacterial activity of Polish melilot honey were investigated for the first time.
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