Abstract
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.
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Abbreviations
- PMSF:
-
phenylmethylsulfonyl fluoride
- PP:
-
polypeptide
- PTM:
-
posttraslational modification
- PTPP:
-
phosphotyrosine polypeptides
- PVDF membranes:
-
polyvinylene difluoride membranes
- TBST:
-
Tris-buffered saline with Tween 20
- TEMED:
-
tetramethylethylenediamine
- TPK:
-
tyrosine protein kinase
- LTP:
-
level of protein phosphorylation on tyrosine
- TPP:
-
tyrosine protein phosphatase
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Original Russian Text © N.V. Petrova, F.G. Karimova, 2011, published in Fiziologiya Rastenii, 2011, Vol. 58, No. 5, pp. 750–757.
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Petrova, N.V., Karimova, F.G. Effects of redox agents on protein tyrosine phosphorylation in pea roots. Russ J Plant Physiol 58, 899–905 (2011). https://doi.org/10.1134/S1021443711050165
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DOI: https://doi.org/10.1134/S1021443711050165