Abstract
The interaction of fractionated poly(acrylic acid)s (PAA) with bovine serum albumin (BSA) has been studied by measuring the hydrolysis rate of p-nitrophenyl acetate catalysed by BSA in the presence of PAA. The binding of PAA with BSA, which prohibits the catalytic action of BSA, increases with increasing molecular weight of PAA. The change in the electronic spectra of BSA-PAA solutions supports this molecular weight dependence. Circular dichroism of BSA shows that the binding of PAA does not induce any conformational change in BSA.
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