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- W1569450367 abstract "The authors report the efficient solubilization and characterization of a Triton X-100 insoluble tyrosine kinase from rat adipocytes. Plasma membranes were prepared from rat epididymal fat pads and were solubilized in 1% Triton X-100. Following centrifugation, the pellet was solubilized for 15 min at 4C using both ionic and non-ionic detergents. Tyrosine kinase activity was measured in the soluble and particulate fractions using the exogenous substrate poly(glu-tyr) in a TCA precipitation assay. Reactions were performed in 50mM Hepes, 10mM MgCl2 and 100 M gamma(TSP)-ATP (10Ci/mmol) at 4C with or without 1mg/ml of the polyaminoacid. Incorporation rates of 100 to 1000 pmol/min/mg were obtained, while endogenous (TSP) incorporation was typically less than 10% of that in the presence of poly(glu-tyr). More than 75% of the tyrosine kinase activity was recovered in the soluble supernatant using this assay methodology. The solubilized tyrosine kinase was found to require MgS or MnS but preferred MgS and was inhibited by high levels of MnS . Kinase activity was strongly inhibited by CaS (>50% at 1mM), NaCl (>50% at 250mM) and NH4SO4 (>50% at 50mM) but was activated by 10 M heparin and 5mM dithiothreitol. These properties distinguish the solubilized tyrosine kinase from other cellular tyrosinemore » kinases.« less" @default.
- W1569450367 created "2016-06-24" @default.
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- W1569450367 date "1987-05-01" @default.
- W1569450367 modified "2023-09-23" @default.
- W1569450367 title "Solubilization and characterization of a novel tyrosine kinase from rat adipocytes" @default.
- W1569450367 hasPublicationYear "1987" @default.
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