Localization-Dependent Regulation of Lymphocyte Tyrosine Phosphatases

  • Christine Stader
  • Hans Werner Hofer
Conference paper
Part of the NATO ASI Series book series (volume 76)


A soluble tyrosine phosphatase isolated from pig spleen was strongly inhibited by nucleic acid and anionic phospholipids (1,2). Potentially, therefore, the enzyme could be regulated by reversible binding to membranes or nucleic acid — containing structures. In order to examine this hypothesis we studied the localization of tyrosine phosphatases in lymphoid cells.


Tyrosine Phosphatase Anionic Phospholipid Reversible Binding Protease Treatment High Molecular Weight Complex 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.





high molecular weight complex


myelin basic protein


phosphotyrosine protein phosphatase


reduced carboxymethylated and maleylated lysozyme


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Copyright information

© Springer-Verlag Berlin Heidelberg 1993

Authors and Affiliations

  • Christine Stader
    • 1
  • Hans Werner Hofer
    • 1
  1. 1.Faculty of BiologyUniversity of KonstanzKonstanzGermany

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