After isolating components 1' and 2 from heat-treated solution of bovine serum albumin (BSA), their interactions with bilirubin were studied under the same conditions as in the previous study. Spectrophotometric and fluorescence measurements were made at pH 7.5 and 25°C.
1) Comparisons were made of
n and
K for components 1' and 2 with those for components N (native BSA). That the highest-affinity binding site for bilirubin on the denatured forms appeared to be damaged slightly.
2) Comparisons were made of values of ε
b(485 nm) for components 1' and 2 with that for component N. The environment of the site for the interaction for the component N differed from that of denatured forms. Those of the site were the same in components 1' and 2.
3) The fluorescence spectrum of the system of component N and bilirubin differed from that of th system of denatured components and bilirubin. The same conclusion as in (2) would thus appear to apply.
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