Localization-Dependent Regulation of Lymphocyte Tyrosine Phosphatases
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.
KeywordsFiltration EDTA Tyrosine Heparin Vanadate
high molecular weight complex
myelin basic protein
phosphotyrosine protein phosphatase
reduced carboxymethylated and maleylated lysozyme
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