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'Phosphorylation' in keywords Facet   Publication Year 1981  [X]
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1Author    Hans-Adolf Arfmann, Hassan BaydounRequires cookie*
 Title    Preferential Phosphorylation of High Mobility Group Protein 17 in vitro by a Nuclear Protein Kinase  
 Abstract    The ability of the high mobility group proteins (H M G -1,2,14 and 17) to serve as substrate for protein kinases was investigated by incubating them with a cytoplasmic and nuclear kinase. In both cases phosphate was incorporated into all four HMG proteins. The amount of phosphate incorporated and the specificity for the four proteins was quite different for the two kinases. Whereas the cytoplasmic kinase phosphorylated the HMG-1 and 2 to a higher degree than HM G -14 and 17, the nuclear kinase exhibited a high specificity for the H M G -17, leaving the other three proteins with only a small amount. The high preference o f a nuclear kinase for HM G-17 may be indicative o f a specific phosphorylation occuring also in vivo. 
  Reference    Z. Naturforsch. 36c, 319—322 (1981); received October 6/November 26 1980 
  Published    1981 
  Keywords    High Mobility Group Proteins, Phosphorylation, Nuclear and Cytoplasmic Kinase 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0319.pdf 
 Identifier    ZNC-1981-36c-0319 
 Volume    36