Abstract
The binding between bilirubin and human serum albumin was studied spectrophotometrically and with Sephadex gel filtration. Spectral absorption curves of solution of bilirubin in buffers containing decreasing amounts of albumin were registered. At a molar bilirubin to albumin ratio of 1:1 a change in these curves takes place, indicating that only one molecule of bilirubin is tightly bound to albumin. Sephadex gel filtration studies also showed that with solution containing bilirubin and albumin in molar ratios above 1:1 bilirubin seemed, however, to be more loosely bound.
The toxic effect of bilirubin on human fibroblasts in tissue culture was also tested. When solutions containing bilirubin to albumin ratios above 1:1 were added to the growth medium, a toxic effects was seen on the fibroblast growth. With a bilirubin to albumin ratio of 2:1 rapid cell death was found with total bilirubin concentrations as low as 5 mg/100 ml. On the other hand, when the bilirubin to albumin ratio in the growth medium was below 1:1, the cells tolerated bilirubin concentrations as high as 20 mg/100 ml, which was the highest tested. It therefore seems that only one molecule of bilirubin is tightly bound to each molecule of albumin, ab\nd that this molecule only is detoxified.
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Bratlid, D., Fog, J. & Lie, S. 54. Binding capacity of human albumin for bilirubin. Pediatr Res 5, 94–95 (1971). https://doi.org/10.1203/00006450-197102000-00059
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DOI: https://doi.org/10.1203/00006450-197102000-00059