Tumor suppressor protein p53 is often expressed as a fusion protein with glutathione-S-transferase (GST). The sensitive determination of GST in p53 samples is thus necessary. We propose a method for the determination of traces of GST in the p53 C-terminus based on the constant current chronopotentiometric stripping analysis (CPSA) with hanging mercury drop electrode (HMDE). GST produces a catalytic signal in cobalt-containing solutions due to cysteine residues. A large excess of the C-terminus does interfere with the determination because of the lack of cysteines in the molecule. This method is simple and very sensitive and is capable of detecting <1% GST in the p53 sample.

Institute of Biophysics Academy of Sciences of the Czech Republic Královopolská 135 CZ 612 65 Brno Czech Republic

Citace poskytuje Crossref.org

Preferential binding of hot spot mutant p53 proteins to supercoiled DNA in vitro and in cells

Change of the protein p53 electrochemical signal according to its structural form - quick and sensitive distinguishing of native, denatured, and aggregated form of the "guardian of the genome"

Role of tumor suppressor p53 domains in selective binding to supercoiled DNA