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Rahman, A.A. and Sharker, S.M. (2009) Determination of the binding sites of propranolol HCl on bovine serum albumin by direct and reverse procedures. Saudi Pharmaceutical Journal, 17, 249-253. doi:10.1016/j.jsps.2009.08.002

has been cited by the following article:

• TITLE: Analysis of the interaction between [Ru(phenanthroline)3]2+ and bovine serum albumin

  AUTHORS: Laura Luzuriaga, María Fernanda Cerdá

  KEYWORDS: Saturation Graph; Spectrophotometry; Cyclic Voltammetry

  JOURNAL NAME: Advances in Biological Chemistry, Vol.2 No.3, August 22, 2012

  ABSTRACT: The interaction of compounds with potential use as pharmaceutical with a carrier protein as serum albumin is of great importance in their biodistribution. Albumin offers different sites for binding metallic compounds. Using a combination of spectropho-tometric and electrochemical techniques, the interaction between [Ru(phen)3]Cl2 (phen = phenantroline) and bovine serum albumin was evaluated. In particular, it was possible to calculate an apparent binding constant (Kb) of 4.4 × 103 (for concentrations expressed in M) for the main interaction site of the protein. A number of ca. 40 molecules of Ru-phen per molecule of BSA under saturation conditions, and a positive cooperative behavior towards association from the protein were found.