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- W2359559151 abstract "Object To study the mechanism of signal transduction in K562 cell differentiation induced by matrine. Methods The method of ELISA coupled with streptaviding biotin system was used to detect the activity of protein tyrosine kinase and phosphatase respectively in cytoplasm and membrane of K562 cells treated by matrine at different time. Results Using specific kinase inhibitor, it was demonstrated in the first time that the activity of protein tyrosine kinase decreased transiently accompanying the change of protein tyrosine phosphatase activity. Conclusion The change of protein tyrosine kinase activity was involved in the course of K562 cell differentiation induced by matrine. The tyrosine kinase activity in cell membrane decreases more rapidly than that in cell cytoplasm, suggesting that there be a signal transmembrane transport process. The change of tyrosine phosphatase activity following the kinase reflects the real time regulation of phosphorylation and dephosphorylation." @default.
- W2359559151 created "2016-06-24" @default.
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- W2359559151 date "2003-01-01" @default.
- W2359559151 modified "2023-09-25" @default.
- W2359559151 title "Change of tyrosine kinase and phosphatase activity in K562 cells induced by matrine" @default.
- W2359559151 hasPublicationYear "2003" @default.
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