Measurement of protein tyrosine phosphatase activity in single cells by capillary electrophoresis.
作者： Ryan M. Phillips , Eric Bair , David S. Lawrence , Christopher E. Sims , Nancy L. Allbritton
DOI: 10.1021/AC401106E
关键词: Enzyme 、 Enzyme activator 、 Chemistry 、 Flow cytometry 、 Phosphatase 、 Substrate (chemistry) 、 Dephosphorylation 、 Protein tyrosine phosphatase 、 Biochemistry 、 PTPN1 、 Molecular biology
摘要: A fluorescent peptide substrate was used to measure dephosphorylation by protein tyrosine phosphatases (PTP) in cell lysates and single cells investigate the effect of environmental toxins on PTP activity these systems. Dephosphorylation PTPN1 PTPN2 obeyed Michaelis–Menten kinetics, with KM values 770 ± 250 290 54 nM, respectively. Dose–response curves IC50 were determined for inhibition two enzymes Zn2+ 1,2-naphthoquinone, as well pervanadate. In A431 lysates, reporter a poor peptidases (degradation rate 100 8.2 fmol min–1 mg–1) but an excellent (dephosphorylation 1.4 0.3 nmol mg–1). Zn2+, pervanadate inhibited 470 35 μM, reporter, following loading into living cells, occurred ...
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