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• W2095251015 abstract "A non-myristylated form (LCKM) of the human T-lymphocyte-specific protein tyrosine kinase (LCK) was produced at high levels in a baculovirus expression system (BVES) using two strategies. First, LCKM was produced by direct expression of a Gly2→ Ala mutant of LCK. Second, LCK was produced as a glutathione S-transferase (GST) fusion, and LCKM was derived from the fusion protein by cleavage with thrombin. Both recombinant proteins (re-proteins) were produced at 5% of the total protein of infected Spodoptera frugiperda (Sf9) cells and were purified to >95% homogeneity. The enzymatic properties of the re-proteins and their inhibition by protein kinase inhibitors were comparable to the native enzyme (LCKN) derived from Jurkat cells and wild-type LCK derived from the BVES. The high production levels will facilitate the recovery of large quantities of re-protein for use in biochemical and biophysical studies" @default.
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• W2095251015 date "1996-01-01" @default.
• W2095251015 modified "2023-09-23" @default.
• W2095251015 title "Production, purification and characterization of non-myristylated human T-cell protein tyrosine kinase in a baculovirus expression system" @default.
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• W2095251015 doi "https://doi.org/10.1016/0378-1119(95)00817-9" @default.
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