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Nuclear translocation of aflatoxin B1 - protein complex
J J Ch'ih1, J I Ewaskiewicz, P Taggart
1Department of Biological Chemistry, Hahnemann University, School of Medicine, Philadelphia, PA 19102-1192.
Biochemical and Biophysical Research Communications
|January 15, 1993
Abstract:
The in vitro binding of [3H]-AFB1 to various proteins was studied by equilibrium dialysis. At 23 +/- 1 degree C, [3H]-AFB1 binding activity (mmol/mol) decreased as follows: pyruvate kinase > albumin-NLS > albumin > carbonic anhydrase > RNase > histones. The nuclear translocation and activation of AFB1 and AFB-protein complexes was investigated using isolated rat liver nuclei in the presence of ATP and a NADPH regenerating system. Proteins containing NLS such as histones and albumin-NLS facilitated AFB1 translocation into the nucleus where activation and adduct formation took place.