Early changes in irradiated solutions of bilirubin were evaluated by spectrophotometric techniques. By absorbance difference (AD) spectroscopy, the photoproducts formed in solutions of bilirubin combined with human serum albumin were found to differ from those formed in naturally or artificially jaundiced rat serum, bovine serum albumin solutions, or chloroform or carbon tetrachloride solutions. With a technique based on variable path‐length compensation for bilirubin loss (compensated absorbance difference or CAD spectroscopy) the approximate shapes of photoproduct absorption spectra could be evaluated. Chloroform and bovine serum albumin solutions produced single‐peaked products absorbing at slightly shorter wavelengths than bilirubin. Human serum albumin solutions produced a twin‐peaked chromophore absorbing most strongly near 490 nm.
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Davies et al. (1973) studied this question.
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