Tyrosinase and superoxide dismutase activities of peroxidase in the vacuoles of beet roots

Tyrosinase and superoxide dismutase activities of peroxidase in the vacuoles of beet roots In the absence of H2O2, isoforms of vacuolar phenol-dependent peroxidase (PO) in beet (Beta vulgaris) roots oxidized phenolic compounds like tyrosinases. Tyrosinase activity of PO manifested a clearly expressed pH-dependence with the optimum at pH of 8.0–9.0; peroxidase activity was the highest at pH 5.0–7.0. The inhibitory analysis confirmed a specificity of observed reactions. Along with tyrosinase activity, PO manifested SOD-like activity, which was also expressed in the absence of H2O2 and depended on some factors, for example, on the way of analyzed sample preparation. This activity appeared at a long-term dialysis and low temperature. SOD-like PO activity was observed in the presence of such substrates as 3,3′-diaminobenzidine and IAA. The results obtained allow a conclusion that vacuolar PO, as well as PO of other localization and origin is a polyfunctional enzyme, which, under definite conditions, can catalyze reactions of oxidase type. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Tyrosinase and superoxide dismutase activities of peroxidase in the vacuoles of beet roots

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Springer US
Copyright © 2014 by Pleiades Publishing, Ltd.
Life Sciences; Plant Physiology; Plant Sciences
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