Protein Phosphorylation in Membranes of Nicotiana Tabacum

  • Klaus Palme
  • Jorge E. Mayer
  • Jeff Schell
Conference paper
Part of the NATO ASI Series book series (NSSA, volume 135)


We have identified growth related changes in phosphoproteins from Nicotiana tabacum membranes. Changes in the phosphorylation patterns suggest that different substrates and different phosphorylation sites in substrates are used. Most remarkably, a change in the phosphorylation of a 33.000 Da phosphoprotein was correlated with the presence of cytokinin-like growth hormones in the culture media. A membrane bound protein kinase with an apparent Mr of 16.500 was isolated from Nicotiana tabacum and purified to homogeneity.


Growth Hormone Platelet Activate Factor Nicotiana Tabacum Phosphorylation Pattern Crude Membrane Fraction 
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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Klaus Palme
    • 1
  • Jorge E. Mayer
    • 1
  • Jeff Schell
    • 1
  1. 1.Max Planck-Institut für ZüchtungsforschungKoln 30Germany

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