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- W2549917967 abstract "Abies (Abies alba Mill) bark agglutinin, AbA2 inhibited the peroxidase from the same tissue up to 35% with an IC50 of 0.763 × 10 -2 M. The Km of free Fir peroxidase was 0.249 × 10 -2 M., while by interaction with 2.1 µg/ml of AbA2 the binding efficiency increases 2 times. The kinetic data of the enzymatic activity of Fir bark peroxidase incubated with the AbA2 lectin (0.6–2.1 µg/ml) showed a mixed type of inhibition (competitive/uncompetitive). At relatively high concentration of AbA2 lectin (2.1 µg/ml) the mixed inhibition type of Fir peroxidase changed to fairly competitive. Hydrolysis of AbA2 lectin and Fir peroxidase with 5% H2SO4, and subsequent dyeing for Fe ions on TLC silicagel plates revealed the existence of Fe 3+ in the structure of both AbA2 lectin and Fir peroxidase. Incubation of AbA2 lectin with EDTA, as possible chelator of Fe 3+ increases the peroxidase inhibition changing the behavior into highly competitive. No modifications in peroxidase activity were shown after incubation of AbA2 lectin (1.2 µg/ml) with 40 mM of GlN, GalN, GlNAc, GalNAc and Fuc The interaction of AbA2 lectin with Fir peroxidase at the protein level through Fe 3+ was discussed." @default.
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- W2549917967 date "2011-01-01" @default.
- W2549917967 modified "2023-09-23" @default.
- W2549917967 title "FIR BARK (ABIES ALBA MILL.) LECTIN IS AN INHIBITOR OF FIR PEROXIDASE IN VITRO" @default.
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