Posttranslational protein modifications and their interaction are an important way for the regulation of activities of proteins and their supramolecular complexes. More than 50 soluble proteins phosphorylated on tyrosine were detected in pea (Pisum sativum L., cv. Truzhenik) roots by one- and two-dimensional electrophoresis and immunoblotting with a highly specific antibody (PY20). The level of tyrosine phosphorylation of these proteins was changed under in situ action of redox and alkylating agents.
Russian Journal of Plant Physiology – Springer Journals
Published: Aug 21, 2011
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