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Experimental study on the interaction between lead and serum albumin
Author(s) -
Zuorro Antonio,
Lavecchia Roberto
Publication year - 2012
Publication title -
asia‐pacific journal of chemical engineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.348
H-Index - 35
eISSN - 1932-2143
pISSN - 1932-2135
DOI - 10.1002/apj.1652
Subject(s) - enthalpy , chemistry , bovine serum albumin , titration , aqueous solution , saturation (graph theory) , thermodynamics , entropy (arrow of time) , langmuir equation , analytical chemistry (journal) , chromatography , langmuir , inorganic chemistry , physics , mathematics , combinatorics
The interaction between lead (Pb 2+ ) and bovine serum albumin (BSA) was studied in the temperature range of 10–40 °C through metal‐titration experiments under equilibrium conditions. Lead binding to BSA was monitored by measuring the intensity changes in the difference absorption band at 243 nm following the addition of increasing amounts of lead ions to an aqueous solution at constant protein concentration (2.5 × 10 −5 M). The equilibrium binding data were found to be well described by a Langmuir‐type equation, with an almost temperature‐independent saturation value. According to the estimated Δ H 0 and Δ S 0 , the binding of Pb 2+ to BSA was both enthalpy‐driven and entropy‐driven, with the entropic contribution providing the major driving force. © 2012 Curtin University of Technology and John Wiley & Sons, Ltd.