Effects of oxidation on changes of compressibility of bovine serum albumin.
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.
Hianik
T
T
Department of Biophysics and Chemical Physics, Faculty of Mathematics, Physics and Computer Science, Comenius University, Bratislava, Slovakia. hianik@fmph.uniba.sk
Rybár
P
P
Benediktyová
Z
Z
Svobodová
L
L
Hermetter
A
A
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
D000578:Amidines; D013535:Suspensions; D012710:Serum Albumin, Bovine; C046728:2,2'-azobis(2-amidinopropane); D003300:Copper