Phosphorylation of proteins in the cultured buckwheat cells differing in morphogenic abilities

Phosphorylation of proteins in the cultured buckwheat cells differing in morphogenic abilities The level of Ca2+-and cAMP-dependent phosphorylation of intracellular and extracellular proteins in morphogenic calli of buckwheat (Fagopyrum tataricum (L.) Gaertn.) was higher than in nonmorphogenic calli. Using monoclonal (PY20) antibodies we showed that morphogenic and nonmorphogenic calli also differed in the number of proteins phosphorylated at tyrosine residues and by the extent of their phosphorylation. As compared with morphogenic calli, nonmorphogenic calli lacked phosphorylation at tyrosine in the protein with molecular weight of 21 kD and manifested reduced phosphorylation of proteins with molecular weights of 19, 22, and 29 kD. This evidence suggests that in the cultured cells incapable of regenerating plants, considerable changes occur in intracellular regulation and intercellular communications. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Phosphorylation of proteins in the cultured buckwheat cells differing in morphogenic abilities

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/lp/springer_journal/phosphorylation-of-proteins-in-the-cultured-buckwheat-cells-differing-N20NZcryJ1
Publisher
SP MAIK Nauka/Interperiodica
Copyright
Copyright © 2010 by Pleiades Publishing, Ltd.
Subject
Life Sciences; Plant Sciences ; Plant Physiology
ISSN
1021-4437
eISSN
1608-3407
D.O.I.
10.1134/S1021443710010061
Publisher site
See Article on Publisher Site

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