Analysis of ligand binding process using binding capacity concept

• Autorzy: Bordbar A. K. , Saadati Z. , Sohrabi N.
• Języki publikacji: EN

Abstrakty

EN

Binding capacity is the homotropic second derivative of the binding potential with respect to the chemical potential of the ligand. It provides a measure of steepness of the binding isotherm and represents the extent of cooperativity. In the present study, the shape of the binding capacity curve for various systems was investigated and the relation between binding capacity and the extent of cooperativity examined. In this regard, a novel linear graphical method was introduced for binding data analysis. The stoichiometry of binding and the extent of cooperativity can be determined by this method. This method has been successfully applied to various systems such as binding of oxygen to hemoglobin, warfarin to human serum albumin and dodecyl- trimethylammonium bromide to a-amylase.

Słowa kluczowe

EN

binding capacity; binding stoichiometry; cooperativity; ligand binding

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2004
• Tom: 51
• Numer: 4
• Opis fizyczny: p.963-970,fig.,ref.

Twórcy

autor

Bordbar A. K.

• Isfahan University, Isfahan, 81746-73441, Iran

autor

Saadati Z.

autor

Sohrabi N.

Bibliografia

• Birkett DJ, Ray S, Sudlow G, Hagedorn J. (1980) Fluorescent probe studies of albumin binding sites. Acta Pharm Suec.; 17: 78.
• Bordbar AK, Saboury AA, Moosavi-Movahedi AA. (1996) The shapes of Scatchard plots for systems with two sets of binding sites. Biochem Edu.; 24: 172-5.
• Bordbar AK, Saboury AA, Hosaindokht AA, Moosavi-Movahedi AA. (1997) Statistical effect to the binding of the ionic surfactant to protein. J Colloid Interface Sci.; 192: 415-9.
• Cera E, Gill S. Wyman J. (1988) Binding capacity: cooperativity and buffering in biopolymers. Proc Natl Acad Sci USA.; 85: 449-52.
• Fehske KJ, Muller WE, Wollert U. (1981) The location of drug binding sites in human serum albumin. Biochem Pharmacol.; 30: 687-92.
• Fehske KJ, Schlafer U, Wollert U, Muller WE. (1982) Characterization of an important drug binding area on human serum albumin including the high-affinity binding sites of warfarin and azapropazone. Mol Pharmacol.; 21: 387-93.
• Gharibi H, Razavizadeh BM, Rafati AA. (1998) Electrochemical studies associated with the micellization of dodecyltrimethyl ammonium bromide (DOTAB) in aqueous solutions of ethanol and 1-propanol. Colloid Surfaces A: Physicochemical and Engineering Aspects.; 136: 123-32.
• Goddard ED. (1993) In: KP. Ananthapadmanabhan, ed. Protein-Surfactant Interactions. CRC Press, Boca Raton, New York.
• Hill AV. (1910) J Physiol.; 40: 4.
• Jones MN. (1975) Biological Interface. Elsevier, Amsterdam.
• Jones MN. (1988) Biological Thermodynamics. Jones MN, ed, p 182, Elsevier, Amsterdam.
• Jones MN, Brass A. (1991) Food Polymers, Gels and Colloids. Royal Society of Chemistry, Cambridge.
• Jones MN. (1992) Surfactant interactions with biomembranes and proteins. Chem Soc Rev.; 21: 127-36.
• Klotz IM, Huston DL. (1975) Protein interaction with small molecules relationships between stoichiometric binding constants, site binding constants, and empirical binding parameters. J Biol Chem.; 250: 3001-9.
• Kruz H. (1986) Methodological Problems in Drug — Binding Studies. In: Reidenberg E, ed. Drug-Protein Binding. New York.
• Scatchard G (1949) The attraction of proteins for small molecules and ions. Ann NY Acad Sci., 51: 660-72. Schellman J. (1975) Macromolecular binding. Biopolymers.; 14: 999-1018. Tanford C. (1993) Physical Chemistry of Macromolecules. Wiley, New York.Villamor JP, Zaton AL. (2001) Data plotting of warfarin binding to human serum albumin. J Biochem Biophys Methods.; 48: 33-41.