It has been stated by McDonagh, Palma & Lightner [(1982) J. Am. Chem. Soc. 104, 6867-6871] that complexing of bilirubin with serum albumin has a marked species-dependent influence on bilirubin photoisomerization in vitro and in vivo. Therefore the kinetics for the quantitatively important reaction: (Formula: see text) of the photochemical interconversion between bilirubin and its photoisomers bound to human or rat serum albumin in aqueous solution, assayed by h.p.l.c., was used to elucidate the observed species-dependent difference. The relative rate constants for bilirubin bound to human serum albumin, except for k4, the rate of interconversion from (ZZ)-bilirubin into (EZ)-bilirubin, proved to be considerably larger than those for bilirubin bound to rat serum albumin. In accordance with these rate constants, the formation of photoisomers of bilirubin bound to human serum albumin, except for (EZ)-bilirubin, is very rapid and much greater than that for bilirubin bound to rat serum albumin.
Comparison of kinetic study of the photochemical changes of (ZZ)-bilirubin IXα bound to human serum albumin with that bound to rat serum albumin
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S Onishi, S Itoh, T Yamakawa, K Isobe, M Manabe, S Toyota, T Imai; Comparison of kinetic study of the photochemical changes of (ZZ)-bilirubin IXα bound to human serum albumin with that bound to rat serum albumin. Biochem J 15 September 1985; 230 (3): 561–567. doi: https://doi.org/10.1042/bj2300561
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