RESUMEN
This study was designed to examine Allium schoenoprasum tissue culture organs antioxidant and scavenging activity and to make a comparison between Allium schoenoprasum cultivated plant and Allium schoenoprasum tissue culture organs antioxidant activity. This study reports the results on the root, stalk and leaf antioxidant enzyme activities (superoxide dismutase, catalase, guaiacol peroxidase and glutathione peroxidase), reduced glutathione quantity, flavonoids and soluble protein contents and quantities of malonyldialdehyde and ·OH radical. In Allium schoenoprasum tissue culture organs the total antioxidant capacity was determined by the FRAP method and scavenger activity by the DPPH method. The present results indicated that the crude extract of Allium schoenoprasum tissue culture exhibited antioxidant and scavenging abilities in all investigated plant parts, especially in the roots. According to our results, the tissue culture plants exhibited the highest activities in the roots in contrast to the cultivated plants where highest activities were observed in the leaves.
Asunto(s)
Antioxidantes/análisis , Cebollino/enzimología , Técnicas de Cultivo de Tejidos , Catalasa/metabolismo , Flavonoides/análisis , Depuradores de Radicales Libres/análisis , Glutatión/análisis , Glutatión Peroxidasa/metabolismo , Óxido Nítrico/metabolismo , Peroxidasa/metabolismo , Hojas de la Planta/metabolismo , Raíces de Plantas/metabolismo , Superóxido Dismutasa/metabolismoRESUMEN
Chives have been used both as food and as medicine. Previously, two fibrinolytic enzymes, ATFE-I (90 kDa) and ATFE-II (55 kDa), were identified in chives (Allium tuberosum), a perennial herb. In the present work, ATFE-II was purified by ion-exchange chromatography followed by gel filtration. In addition, the enzyme properties of ATFE-I and ATFE-II were compared. The molecular mass and isoelectric point (pI value) of ATFE-II were 55 kDa and pI 4.0, respectively, as revealed using one- or two-dimensional fibrin zymography. ATFE-II was optimally active at pH 7.0 and 45°C. ATFE-II degraded the Aα-chain of human fibrinogen but did not hydrolyze the Bß-chain or the γ-chain, indicating that the enzyme is an α-fibrinogenase. The proteolytic activity of ATFE-II was completely inhibited by 1 mM leupeptin, indicating that the enzyme belongs to the cysteine protease class. ATFE-II was also inhibited by 1 mM Fe²(+). ATFE-II exhibited high specificity for MeO-Suc-Arg-Pro-Tyr-p-nitroaniline (S-2586), a synthetic chromogenic substrate of chymotrypsin. Thus proteolytic enzymes from A. tuberosum may be useful as thrombolytic agents.