Certain concentrations of the cold-shock protein (CSP310) were shown to induce systems of lipid peroxidation (POL) in winter wheat (Triticum aestivum L.) mitochondria in vitro. The process of nonenzymatic POL turned out to be the most sensitive to the presence of CSP310 in the incubation medium. The maximum induction of the enzymatic POL occurred at a higher CSP310 concentration. Wheat, maize (Zea mays L.), and elymus (Elymus sibiricus L.) proteins, which are immunochemically related to CSP310, did not manifest prooxidant properties, and, moreover, the elymus proteins had a clear-cut antioxidant effect. At the same time, these proteins uncoupled oxidation and phosphorylation to a far lesser extent than the winter rye (Secale cereale L.) CSP310. During low-temperature stress, the activation of uncoupling systems of wheat mitochondria by pyruvate, linoleic acid, and CSP310 was accompanied by an increase in oxygen consumption by seedlings and a decrease in the POL level.
Russian Journal of Plant Physiology – Springer Journals
Published: Oct 13, 2004
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