title: Effects of oxidation on changes of compressibility of bovine serum albumin.
abstract: The methods of ultrasound velocity and density measurements were used to study the adiabatic compressibility of bovine serum albumin (BSA) during its oxidation by the prooxidants Cu2+ and 2,2'-azobis(2-amidinopropane) hydrochloride (AAPH). We did not find changes of compressibility of BSA in the presence of copper ions at rather high molar ratio Cu2+/BSA = 0.66 mol/mol. This can be explained by binding of the Cu2+ to the binding site of BSA and thus protecting the prooxidant action of the copper. However, AAPH-mediated oxidation of BSA resulted in an increase of its apparent specific compressibility (psik/beta0). These changes could be caused by the fragmentation of the protein.
authors.affiliation: Department of Biophysics and Chemical Physics, Faculty of Mathematics, Physics and Computer Science, Comenius University, Bratislava, Slovakia. hianik@fmph.uniba.sk
authors.forename: T
authors.initials: T
authors.lastname: Hianik
authors.forename: P
authors.initials: P
authors.lastname: Rybár
authors.forename: Z
authors.initials: Z
authors.lastname: Benediktyová
authors.forename: L
authors.initials: L
authors.lastname: Svobodová
authors.forename: A
authors.initials: A
authors.lastname: Hermetter
mesh_terms: D000578:Amidines / Q000737:chemistry*; D003300:Copper / Q000737:chemistry*; D003720:Densitometry / Q000379:methods; D004548:Elasticity; D010084:Oxidation-Reduction; D012710:Serum Albumin, Bovine / Q000032:analysis / Q000737:chemistry*; D013535:Suspensions / Q000737:chemistry; D014463:Ultrasonography / Q000379:methods
chemical_list: D000578:Amidines; D013535:Suspensions; D012710:Serum Albumin, Bovine; C046728:2,2'-azobis(2-amidinopropane); D003300:Copper