title: Thiophilic interaction chromatography of serum albumins.
abstract: 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.
authors.affiliation: Department of Cancer Biology, Roswell Park Cancer Institute, Buffalo, NY 14263, USA.
authors.forename: Mustapha
authors.initials: M
authors.lastname: Bourhim
authors.forename: Anita
authors.initials: A
authors.lastname: Rajendran
authors.forename: Yanira
authors.initials: Y
authors.lastname: Ramos
authors.forename: Thamarapu
authors.initials: T
authors.lastname: Srikrishnan
authors.forename: Eugene
authors.initials: E
authors.lastname: Sulkowski
mesh_terms: D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D006801:Humans; D011994:Recombinant Proteins / Q000737:chemistry; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet
chemical_list: D011994:Recombinant Proteins; D012709:Serum Albumin