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Luminescence Resonance Energy Transfer to Study Conformational Changes in Membrane Proteins Expressed in Mammalian Cells
Published on: September 16, 2014
Sensitive determination of proteins by its quenching effect on fluorescence of new terbium(III) complex
Inna Leonenko1, Daria Aleksandrova, Alla Yegorova
1A. V. Bogatsky Physico-Chemical Institute of National Academy of Sciences of Ukraine, Odessa 65080, Ukraine.
Abstract:
It is found that in hexamethylenetetramine (HMTA-HCl) buffer pH = 7.8, proteins can quench the fluorescence intensity of new terbium(III) complex with 6-[(1-hydroxy-3-oxo-6,7-dihydro-3H,5H-pyrido[3,2,1-ij]quinoline-2-carbonyl)-amino]-hexanoic acid (L). Based on this, a sensitive fluorimetric method for the determination of proteins is proposed. Under optimum conditions, the I0/I is in proportion to the concentration of protein in the range of 0.1-40.0 microg/mL for bovine serum albumin (BSA), 0.1-70.0 microg/mL for human serum albumin (HSA) and 0.1-40.0 microg/mL for immunoglobulin G (IgG). Their detection limits (S/N = 3) are 0.03 microg/mL. The interaction mechanism for the luminescence quenching is also studied.
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