Molecular and Cellular Biochemistry

, Volume 277, Issue 1, pp 101–107

Interaction of bilirubin with sealed and human serum albumin-entrapped sealed membranes


  • Huma Rashid
    • Interdisciplinary Biotechnology UnitAligarh Muslim University
  • Mohammad Mushahid Khan
    • Interdisciplinary Biotechnology UnitAligarh Muslim University
    • Department of Neurology, School of MedicineThe Medical College of Georgia
    • Interdisciplinary Biotechnology UnitAligarh Muslim University
    • Insitut Sains BiologiUniversiti Malaya

DOI: 10.1007/s11010-005-5425-6

Cite this article as:
Rashid, H., Khan, M.M. & Tayyab, S. Mol Cell Biochem (2005) 277: 101. doi:10.1007/s11010-005-5425-6


In order to study the mechanism of entry and localization of bilirubin (BR) into cell membrane, binding of BR to sealed and human serum albumin (HSA)-entrapped sealed membranes was studied by CD spectroscopy. An induced bisignate CD cotton effects (CDCEs) of BR-bound sealed membranes were observed with maxima at 515 nm and minima at 470 nm with a shoulder at 430 nm. BR-bound HSA-entrapped sealed membranes produced CD spectra with additional positive peaks at 450 and 475 nm and negative troughs at 390 and 415 nm. The induced CDCEs of BR-bound sealed membranes and BR-bound HSA-entrapped sealed membranes were perturbed by the addition of drugs (ceftriaxone and sodium salicylate) with the effect of ceftriaxone being more pronounced. Drugs’ being the displacer of BR from albumin, their incorporation in the incubation mixture was paralleled by reduction in CDCEs. Taken together, these results suggest that BR can traverse the membrane bilayer towards the inner surface instead of remaining intercalated in the exterior half of the bilayer.


bilirubin-albumin interactionbilirubin bindingCD spectroscopydrug-induced bilirubin displacementhuman erythrocyte membrane
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© Springer Science + Business Media, Inc. 2005