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Adsorption of bilirubin of polymer sorbents

Adsorption of bilirubin from aqueous buffer (pH = 7.8) by PVP, by cholestyramine and by amino acid containing pendants, which have been immobilized onto a polystyrene (Merrifield) resin or a water swellable polyamide resin using the solid phase peptide synthesis methods, have been studied. The adsorption of bilirubin by the pendants on the Merrifield resin was minimal while PVP and cholestyramine adsorbed some bilirubin. However, the best adsorbents were the immobilized amino acids on a water swellable polyamide resin. / A systematic study of the effect of the changes in the amino acid composition of the pendant, both in type and number, on the adsorption by the polyamide resins indicates that the change density, contributed by the R groups of the amino acids in the pendant, is the major factor in the adsorption process. However, some adsorption also occurs at the (alpha)-amino groups. Effects due to the conformation of the peptide chains are also indicated. Of the resins studied, those with peptide pendants containing arginine or lysine form the most efficient adsorbents for bilirubin in aqueous buffer solution. / Studies of the adsorption of bilirubin from bilirubin solutions containing bovine serum albumin as well as studies of desorption of bilirubin from the resins by bovine serum albumin indicates that some resins containing arginine in the pendants can successfully compete with albumin. Stoichiometric binding constants obtained for the polyamide resins by the method of Klotz are of the order of 1 x 10('3) M('-1) to 86 x 10('3) M('-1). These binding constants are lower than that of the reported values for the first binding site of bilirubin on albumin by a factor of 10('1) to 10('4) and lower by a factor of 10 to 10('3) than the values reported for the second binding site.

Identiferoai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.72026
Date January 1985
CreatorsHenning, D. S., (Dominique S.)
PublisherMcGill University
Source SetsLibrary and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada
LanguageEnglish
Detected LanguageEnglish
TypeElectronic Thesis or Dissertation
Formatapplication/pdf
CoverageDoctor of Philosophy (Department of Chemistry.)
RightsAll items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated.
Relationalephsysno: 000227259, proquestno: AAINL24020, Theses scanned by UMI/ProQuest.

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