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Interaction of bilirubin with native and protein-depleted human erythrocyte membranes

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Vascular Biochemistry

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Abstract

In order to study the role of membrane proteins in bilirubin (BR) binding phenomenon, selective removal of membrane proteins was carried out using various reagents, namely, ethylenediamine tetraacetic acid (EDTA), sodium hydroxide (NaOH), 3,5-diiodosalicylic acid, lithium salt (LIS), dimethylmaleic anhydride (DMMA), sodium iodide (NaI), o-phenanthroline-cupric sulfate (CuP) and phenanthroline-cupric sulfate containing 2-mercaptoethanol (CuP-mercaptoethanol). Effects of these treatments on the conformation and BR binding properties of the membrane were studied using circular dichroism (CD) spectroscopy as well as estimation of membrane-bound BR by diazotised-color reaction. Though a significant amount of protein (ranging from 23-69%) was lost from the membranes upon these treatments, only a small decrease (3-13%) was observed in BR binding, being maximum with NaOH-treated membranes. However, DMMA and NaI treatments produced a little increase in BR binding. Conformation of the membrane was retained to a significant extent as indicated by far-UV CD spectra upon these treatments except in DMMA and Nat treatments which resulted in the perturbation in CD spectra. Taken together, these results suggest that membrane proteins play little role in BR binding, rather act as barriers in BR binding phenomenon. (Mol Cell Biochem 246: 171–177, 2003)

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Authors and Affiliations

  1. Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India

    Huma Rashid & Saad Tayyab

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  1. Huma Rashid
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  2. Saad Tayyab
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Editors and Affiliations

  1. Research Center, St. Boniface General Hospital, 351 Tache Avenue, Winnipeg, Manitoba, R2H 2A6, Canada

    Peter Zahradka

  2. Institute of Cardiovascular Sciences, St. Boniface General Hospital, 351 Tache Avenue, Winnipeg, Manitoba, R2H 2A6, Canada

    Jeffrey Wigle

  3. Division of Stroke & Vascular Disease, St. Boniface General Hospital Research Center, Canada

    Grant N. Pierce

  4. Faculty of Medicine, University of Manitoba, R2H 2A6, Winnipeg, Manitoba, Canada

    Grant N. Pierce

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© 2003 Springer Science+Business Media Dordrecht

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Rashid, H., Tayyab, S. (2003). Interaction of bilirubin with native and protein-depleted human erythrocyte membranes. In: Zahradka, P., Wigle, J., Pierce, G.N. (eds) Vascular Biochemistry. Molecular and Cellular Biochemistry: An International Journal for Chemical Biology in Health and Disease, vol 41. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0298-2_24

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  • DOI: https://doi.org/10.1007/978-1-4615-0298-2_24

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-5010-1

  • Online ISBN: 978-1-4615-0298-2

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