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- W2010697345 abstract "A continuous activity assay for protein tyrosine phosphatases (PTPs), employing phosphotyrosine (P-Tyr) as a substrate, has been developed and applied to measure the activities of two purified enzymes, namely, the full length T-cell protein tyrosine phosphatase (TC PTP) and its truncated form (TCΔC11 PTP). The reaction was followed by changes in ultraviolet absorption and fluorescence resulting from the dephosphorylation of P-Tyr. Both enzymes obey Michaelis-Menten kinetics, with Km = 304 μm, Vmax = 62,000 units/mg for TC PTP and Km = 194 μm, Vmax = 73,000 units/mg for TCΔC11 PTP. The d- and l-forms of P-Tyr are equally effective as substrates. The optimum pH for both enzymes is 4.75. The known effectors of PTPs have the predicted effects on catalytic activity." @default.
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- W2010697345 date "1992-05-01" @default.
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- W2010697345 title "Continuous spectrophotometric assay of protein tyrosine phosphatase using phosphotyrosine" @default.
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- W2010697345 doi "https://doi.org/10.1016/0003-2697(92)90119-r" @default.
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