Journal Article

Thiophilic Interaction Chromatography of Serum Albumins

Mustapha Bourhim, Anita Rajendran, Yanira Ramos, Thamarapu Srikrishnan and Eugene Sulkowski

in Journal of Chromatographic Science

Volume 46, issue 6, pages 574-576
Published in print July 2008 | ISSN: 0021-9665
Published online July 2008 | e-ISSN: 1945-239X | DOI: https://dx.doi.org/10.1093/chromsci/46.6.574

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An investigation of the binding of native and recombinant human serum albumin and bovine serum albumin on three thiophilic gels, PyS, 2S, and 3S was performed. In addition to these proteins, we studied serum albumins from several species such as goat, rabbit, guinea pig, rat, hamster, baboon, and pig. Our results reveal that recombinant human serum albumin (rHSA) binds completely to PyS whereas native human serum albumin and bovine serum albumin bind only partially to PyS. The binding affinities of rHSA, human serum albumin and bovine serum albumin to 2S and 3S gels are less than their binding to PyS. Serum albumins from goat, rabbit, guinea pig, rat, hamster, baboon, and pig bind much stronger to 3S gel than human and bovine serum albumins. The binding of pig and hamster serum albumins is stronger than that of rat, goat, baboon, and rabbit.

Journal Article.  0 words. 

Subjects: Chemistry