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Association Constants in the Bovine Serum Albumin/Human Serum Albumin–Tween 20 System in Aqueous Solutions

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Abstract

The association constants in the bovine serum albumin/human serum albumin–Tween 20 system are determined in aqueous solutions at pH 3.5–8.0 by means of nonpolarized fluorescence and protein fluorescence quenching. It is found that the most efficient association of serum albumin molecules with Tween 20 micelles occurs at pH 5.0 near the isoelectric points of proteins.

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Authors and Affiliations

  1. Faculty of Physics, Moscow State University, Moscow, 119991, Russia

    I. M. Vlasova, A. A. Vlasov, G. R. Grapendaal & A. M. Saletskii

  2. Center for Theoretical Problems of Physicochemical Pharmacology, Russian Academy of Sciences, Moscow, 119991, Russia

    I. M. Vlasova

Authors
  1. I. M. Vlasova
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  2. A. A. Vlasov
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  3. G. R. Grapendaal
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  4. A. M. Saletskii
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Correspondence to A. A. Vlasov.

Additional information

Original Russian Text © I.M. Vlasova, A.A. Vlasov, G.R. Grapendaal, A.M. Saletskii, 2018, published in Zhurnal Fizicheskoi Khimii, 2018, Vol. 92, No. 4, pp. 604–608.

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Vlasova, I.M., Vlasov, A.A., Grapendaal, G.R. et al. Association Constants in the Bovine Serum Albumin/Human Serum Albumin–Tween 20 System in Aqueous Solutions. Russ. J. Phys. Chem. 92, 714–718 (2018). https://doi.org/10.1134/S0036024418040325

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  • DOI: https://doi.org/10.1134/S0036024418040325

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