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• W2059664212 abstract "Live T. cruzi trypomastigotes and amastigotes possess ecto-protein tyrosine phosphatase activity as indicated by the ability of intact cells to catalyze dephosphorylation of tyrosine phosphorylated myelin basic protein, [32P]TyrRaytide, phosphotyrosine, or the phosphotyrosine analog p-nitrophenylphosphate (p-NPP). The dephosphorylation of myelin basic protein (MBP) and p-NPP was inhibited by sodium o-vanadate, zinc chloride and NaF, while dephosphorylation of [32P]TyrRaytide was insensitive to zinc chloride but sensitive to o-vanadate and NaF. In contrast, live cells were not able to dephosphorylate serine or threonine phosphorylated peptides ([32P]Kemptide) or proteins ([32P]RCM-lysozyme and [32P]MBP)." @default.
• W2059664212 created "2016-06-24" @default.
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• W2059664212 date "1998-05-01" @default.
• W2059664212 modified "2023-09-30" @default.
• W2059664212 title "Ecto-protein tyrosine phosphatase activity in Trypanosoma cruzi infective stages" @default.
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• W2059664212 doi "https://doi.org/10.1016/s0166-6851(97)00246-6" @default.
• W2059664212 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9657337" @default.
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