Arch Biochem Biophys. 1992 Nov 1;298(2):710-4.

Conformation inversion of bilirubin formed by reduction of the biliverdin-human serum albumin complex: evidence from circular dichroism.

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Departament de Química Orgànica, Universitat de Barcelona, Catalunya, Spain.

Abstract

As shown by circular dichroism spectroscopy, biliverdin preferentially adopts an M-helicity conformation on human serum albumin in aqueous buffer, pH 7.5, whereas biliverdin exhibits only a weak preference for the P-helicity conformation on bovine serum albumin at the same pH. Upon rapid reduction of the complexes with sodium borohydride, P-helicity bilirubin-IX alpha is obtained on the human albumin complex, and M-helicity bilirubin-IX alpha is obtained on the bovine serum albumin complex. Thus, biliverdin in effect undergoes an inversion of chirality upon reduction. Since the reduction did not afford a rubin with the same helicity as that of the verdin, the observations point to a hitherto undetected conformational mobility of albumin-bound bilirubin.

PMID:: 1416999; [PubMed - indexed for MEDLINE]

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Conformation inversion of bilirubin formed by reduction of the biliverdin-human ...
Conformation inversion of bilirubin formed by reduction of the biliverdin-human serum albumin complex: evidence from circular dichroism.
Arch Biochem Biophys. 1992 Nov 1 ;298(2):710-4.

PubMed
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Conformation inversion of bilirubin formed by reduction of the biliverdin-human serum albumin complex: evidence from circular dichroism.

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