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. 1986 Jun 1;236(2):365-9.
doi: 10.1042/bj2360365.

Conformational changes in the bilirubin-human serum albumin complex at extreme alkaline pH

B Honoré, P C Frandsen

Conformational changes in the bilirubin-human serum albumin complex at extreme alkaline pH

B Honoré et al. Biochem J. .

Abstract

Light-absorption, c.d. and fluorescence of the bilirubin-albumin complex were investigated at extreme alkaline pH. Above pH 11.1 albumin binds the bilirubin molecule, twisted oppositely to the configuration at more neutral pH. On the basis of light-absorption it is shown that two alkaline transitions occur. The first alkaline transition takes place at pH between 11.3 and 11.8, co-operatively dissociating at least six protons. The second alkaline transition takes place at pH between 11.8 and 12.0. It probably implies a reversible unfolding of the albumin molecule, increasing the distance between tryptophan-214 and bilirubin, and partly exposing the liganded bilirubin to the solvent.

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