Abstract
The magnitude and sign of the characteristic circular dichroism spectrum of bilirubin bound to human serum albumin are highly sensitive to the presence of trace amounts of dissolved chloroform. The presence of b-40 mM chloroform in an aqueous solution containing 0.25 mM bilirubin and 0.44 mM albumin is sufficient to cause complete inversion of the circular dichroism curve obtained without chloroform. Addition of chloroform to the albumin solution before or after the bilirubin has the same effect. The sign inversion is not due to a chemical reaction because it was reversed completely on removal of chloroform, regenerating curves characteristic of chloroform-free solutions
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