Go toArchive
Browse byFacets
Bookbag ( 0 )
'Pisum sativum' in keywords Facet   Publication Year 1986  [X]
Results  1 Item
Sorted by   
Section
Publication Year
1986[X]
1Author    Ruth Hracky, Jürgen SollRequires cookie*
 Title    Protein Phosphorylation — Dephosphorylation in the Cytosol of Pea Mesophyll Cells  
 Abstract    Soluble protein kinase and protein phosphatase activities were localized in the cytosol of pea mesophyll cells using protoplasts fractionation techniques. The molecular weights of the phos-phorylated cytosolic proteins, as determined by polyacrylamide gel electrophoresis, were 68, 55, 46, 38, 36, 30, 22 and 12 kDa. Histone and, to a much lesser extent, casein but not phosvitin were accepted as exogenous substrates. In every case serine served as acceptor amino acid for the phosphate residue. The protein phosphorylation activity had an alkaline pH optimum, and showed no response to varying Mg2+, Ca2+, Pn cyclo-AMP or calmodulin concentrations. The kinase activity was competitively inhibited by ADP and pyrophosphate with apparent K t values of 0.5 and 0.17 m M , respectively. High ATP concentrations (1 -4 m M) resulted in a strong decrease of radioactivity in the ,2P labeled proteins. It is proposed that the ratio of protein phosphorylation to protein dephosphorylation is regulated by the ATP to ADP ratio in the cytosol. 
  Reference    Z. Naturforsch. 41c, 856 (1986); received July 9/August 5 1986 
  Published    1986 
  Keywords    Protein Kinase, Protein Phosphatase, Cytosol, Protoplasts, Pisum sativum 
  Similar Items    Find
 DEBUG INFO      
 TEI-XML for    default:Reihe_C/41/ZNC-1986-41c-0856.pdf 
 Identifier    ZNC-1986-41c-0856 
 Volume    41