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- W2018683188 abstract "Native bovine serum albumin (native BSA) was denatured at 65°C for 90 min. Polyacrylamide gel electrophoresis revealed that new components of 1′ (modified monomer) and 2 (dimer of 1′) were formed in the heat-denatured BSA accompanying a drastic decrease in the component 1 (monomer) content. The adsorbability of native and heat-denatured BSA onto hydrophilic polymer latices, particularly onto styrene/acrylamide copolymer [P (St/AAm)] latex, was considerably smaller than that onto polystyrene (PS) latex. The amount of heat-denatured BSA adsorbed onto polymer latices was much greater than that of native BSA, furthermore the pH at maximum adsorption for heat-denatured BSA shifted to a more alkaline pH region compared with that for native BSA. These phenomena were most significantly observed in the adsorption onto PS latex. The analysis by densitometry showed that denatured components (viz., 1′and 2; more hydrophobic than 1) adsorbed preferentially onto PS latex compared with the (undenatured) component 1. It seemed that this preferential adsorption of denatured components contributed to the above-mentioned greater adsorption and the shift of the pH at maximum adsorption for heat-denatured BSA." @default.
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- W2018683188 title "Adsorption of heat-denatured albumin onto polymer latices" @default.
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- W2018683188 doi "https://doi.org/10.1016/0021-9797(88)90121-x" @default.
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